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Volumn 16, Issue 6, 2006, Pages 517-532

Indigenous enzymes in milk: Overview and historical aspects - Part 2

Author keywords

Acid phosphatase; Alkaline phosphatase; Enzymes; Glutathione peroxidase; Lysozyme; Milk; N acetylglucosaminidase; Ribonuclease; Sulphydryl oxidase; Superoxide dismutase

Indexed keywords

ACIDS; ALKALINITY; DAIRIES; ENZYMES; ESTERS; RNA;

EID: 33645393430     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2005.09.017     Document Type: Conference Paper
Times cited : (95)

References (192)
  • 3
    • 84976017382 scopus 로고
    • Bovine milk phosphatase. II. Binding to casein substrates and heat-inactivation studies
    • A.T. Andrews Bovine milk phosphatase. II. Binding to casein substrates and heat-inactivation studies Journal of Dairy Research 41 1974 229 237
    • (1974) Journal of Dairy Research , vol.41 , pp. 229-237
    • Andrews, A.T.1
  • 4
    • 0017087005 scopus 로고
    • Bovine milk acid phosphatase. III. Purification and characterization of the enzyme
    • A.T. Andrews Bovine milk acid phosphatase. III. Purification and characterization of the enzyme Biochimica et Biophysica Acta 434 1976 345 353
    • (1976) Biochimica et Biophysica Acta , vol.434 , pp. 345-353
    • Andrews, A.T.1
  • 5
    • 84971947684 scopus 로고
    • The acid phosphatases of bovine leucocytes, plasma and the milk of healthy and mastitic cows
    • A.T. Andrews, and E. Alichanidis The acid phosphatases of bovine leucocytes, plasma and the milk of healthy and mastitic cows Journal of Dairy Research 42 1975 391 400
    • (1975) Journal of Dairy Research , vol.42 , pp. 391-400
    • Andrews, A.T.1    Alichanidis, E.2
  • 6
    • 84974232170 scopus 로고
    • A study of the heat stabilities of a number of indigenous milk enzymes
    • A.T. Andrews, M. Anderson, and P.W. Goodenough A study of the heat stabilities of a number of indigenous milk enzymes Journal of Dairy Research 54 1987 237 246
    • (1987) Journal of Dairy Research , vol.54 , pp. 237-246
    • Andrews, A.T.1    Anderson, M.2    Goodenough, P.W.3
  • 7
    • 0015897483 scopus 로고
    • Bovine milk acid phosphatase. I. Some kinetic studies and other properties using a partially purified preparation
    • A.T. Andrews, and C. Pallavicini Bovine milk acid phosphatase. I. Some kinetic studies and other properties using a partially purified preparation Biochimica et Biophysica Acta 321 1973 197 209
    • (1973) Biochimica et Biophysica Acta , vol.321 , pp. 197-209
    • Andrews, A.T.1    Pallavicini, C.2
  • 9
    • 0031691978 scopus 로고    scopus 로고
    • The ribonuclease superfamily
    • Anonymous
    • Anonymous The ribonuclease superfamily Cellular and Molecular Life Science 54 1998 763 832
    • (1998) Cellular and Molecular Life Science , vol.54 , pp. 763-832
  • 10
    • 0032857128 scopus 로고    scopus 로고
    • Study of methods to routinely monitor heat load to cheese milk
    • Y. Ardo, O. Lindblad, and K.B. Qvist Study of methods to routinely monitor heat load to cheese milk International Dairy Journal 9 1999 547 552
    • (1999) International Dairy Journal , vol.9 , pp. 547-552
    • Ardo, Y.1    Lindblad, O.2    Qvist, K.B.3
  • 12
    • 0026326603 scopus 로고
    • Partial sequence of human plasma glutathione peroxidase and immunologic identification of milk glutathione peroxidase as the plasma enzyme
    • N. Avissar, J.R. Slemmon, I.S. Palmer, and H.J. Cohen Partial sequence of human plasma glutathione peroxidase and immunologic identification of milk glutathione peroxidase as the plasma enzyme Journal of Nutrition 121 1991 1243 1249
    • (1991) Journal of Nutrition , vol.121 , pp. 1243-1249
    • Avissar, N.1    Slemmon, J.R.2    Palmer, I.S.3    Cohen, H.J.4
  • 15
    • 0018436148 scopus 로고
    • γ-Glutamyl transpeptidase of bovine milk membranes: Distribution and characterization
    • C.R. Baumrucker γ-Glutamyl transpeptidase of bovine milk membranes: Distribution and characterization Journal of Dairy Science 62 1979 253 258
    • (1979) Journal of Dairy Science , vol.62 , pp. 253-258
    • Baumrucker, C.R.1
  • 16
    • 0018853756 scopus 로고
    • Purification and identification of γ-glutamyl transpeptidase of milk membranes
    • C.R. Baumrucker Purification and identification of γ-glutamyl transpeptidase of milk membranes Journal of Dairy Science 63 1980 49 54
    • (1980) Journal of Dairy Science , vol.63 , pp. 49-54
    • Baumrucker, C.R.1
  • 17
    • 0017939972 scopus 로고
    • γ-Glutamyl transpeptidase in lactating mammary secretory tissue of cow and rat
    • C.R. Baumrucker, and P.A. Pocius γ-Glutamyl transpeptidase in lactating mammary secretory tissue of cow and rat Journal of Dairy Science 61 1978 309 314
    • (1978) Journal of Dairy Science , vol.61 , pp. 309-314
    • Baumrucker, C.R.1    Pocius, P.A.2
  • 18
    • 9744221549 scopus 로고    scopus 로고
    • Ribonuclease
    • J.R. Whitaker A.G.J. Voragen D.W.S. Wong Marcel Dekker New York, USA
    • J.J. Beintema, and W. Zhao Ribonuclease J.R. Whitaker A.G.J. Voragen D.W.S. Wong Handbook of food enzymology 2003 Marcel Dekker New York, USA 979 991
    • (2003) Handbook of Food Enzymology , pp. 979-991
    • Beintema, J.J.1    Zhao, W.2
  • 19
    • 1042279556 scopus 로고    scopus 로고
    • Antimicrobial activity of camel's milk against pathogenic strains of Escherichia coli and Listeria monocytogenes
    • N. Benkerroum, M. Mekkaoui, N. Bennani, and K. Hildane Antimicrobial activity of camel's milk against pathogenic strains of Escherichia coli and Listeria monocytogenes International Journal of Dairy Technology 57 2004 39 43
    • (2004) International Journal of Dairy Technology , vol.57 , pp. 39-43
    • Benkerroum, N.1    Mekkaoui, M.2    Bennani, N.3    Hildane, K.4
  • 20
    • 0027013659 scopus 로고
    • Purification and properties of alkaline phosphatase in the lactating bovine mammary gland
    • E.W. Bingham, K. Garver, and D. Powlem Purification and properties of alkaline phosphatase in the lactating bovine mammary gland Journal of Dairy Science 75 1992 3394 3401
    • (1992) Journal of Dairy Science , vol.75 , pp. 3394-3401
    • Bingham, E.W.1    Garver, K.2    Powlem, D.3
  • 23
    • 0026710226 scopus 로고
    • Alkaline phosphatase in the lactating bovine mammary gland and the milk fat globule membrane. Release by phosphatidylinositol-specific phospholipase C
    • E.W. Bingham, and E.L. Malin Alkaline phosphatase in the lactating bovine mammary gland and the milk fat globule membrane. Release by phosphatidylinositol-specific phospholipase C Comparative Biochemistry and Physiology B. Comparative Biochemistry 102 1992 213 218
    • (1992) Comparative Biochemistry and Physiology B. Comparative Biochemistry , vol.102 , pp. 213-218
    • Bingham, E.W.1    Malin, E.L.2
  • 27
    • 37049058324 scopus 로고
    • Structure of lysozyme. a Fourier map of the electron density at 6 Å resolution obtained by X-ray diffraction
    • C.C.F. Blake, R.H. Fenn, A.C.T. North, D.C. Phillips, and R.J. Poljak Structure of lysozyme. A Fourier map of the electron density at 6 Å resolution obtained by X-ray diffraction Nature 196 1965 1173 1176
    • (1965) Nature , vol.196 , pp. 1173-1176
    • Blake, C.C.F.1    Fenn, R.H.2    North, A.C.T.3    Phillips, D.C.4    Poljak, R.J.5
  • 28
    • 28844456836 scopus 로고
    • Lesa proteins du lait, activate enzymatique et hormonal
    • B. Blance Lesa proteins du lait, activate enzymatique et hormonal Lait 62 1982 352 395
    • (1982) Lait , vol.62 , pp. 352-395
    • Blance, B.1
  • 29
    • 0005937656 scopus 로고
    • Le pouvoir bacteriolytique du colostrum et du lait
    • J. Bordet, and M. Bordet Le pouvoir bacteriolytique du colostrum et du lait Comptes Rendus 179 1924 1109 1113
    • (1924) Comptes Rendus , vol.179 , pp. 1109-1113
    • Bordet, J.1    Bordet, M.2
  • 30
    • 33645398433 scopus 로고
    • L'Enzymogramme de la phosphatase alcaline du lait de vache et sa modification pendant le metissage
    • L.M. Buruiana, and M. Marin L'Enzymogramme de la phosphatase alcaline du lait de vache et sa modification pendant le metissage Lait 49 1969 1 8
    • (1969) Lait , vol.49 , pp. 1-8
    • Buruiana, L.M.1    Marin, M.2
  • 31
    • 0015244379 scopus 로고
    • Isolation and partial characterization of lysozyme from baboon milk
    • D.H. Buss Isolation and partial characterization of lysozyme from baboon milk Biochemica et Biophysica Acta 236 1971 587 592
    • (1971) Biochemica et Biophysica Acta , vol.236 , pp. 587-592
    • Buss, D.H.1
  • 32
    • 0024709802 scopus 로고
    • Some comments on the type references of the official nomenclature (IUB) for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase
    • J.C. Cabezas Some comments on the type references of the official nomenclature (IUB) for β-N-acetylglucosaminidase, β-N- acetylhexosaminidase and β-N-acetylgalactosaminidase Biochemical Journal 261 1989 1059 1061
    • (1989) Biochemical Journal , vol.261 , pp. 1059-1061
    • Cabezas, J.C.1
  • 35
  • 38
    • 33645412454 scopus 로고
    • Studies on alkaline milk phosphatase. III. a theory for the mechanism of reactivation of alkaline milk phosphatase in a model system
    • J.W. Copius Peereboom Studies on alkaline milk phosphatase. III. A theory for the mechanism of reactivation of alkaline milk phosphatase in a model system Fette Seifen Anstrichmittel 72 1970 299 308
    • (1970) Fette Seifen Anstrichmittel , vol.72 , pp. 299-308
    • Copius Peereboom, J.W.1
  • 42
    • 0023357779 scopus 로고
    • Selenium content and distribution of human, cow and goat milk
    • B. Debski, M.F. Picciano, and J.A. Milner Selenium content and distribution of human, cow and goat milk Journal of Nutrition 117 1987 1091 1097
    • (1987) Journal of Nutrition , vol.117 , pp. 1091-1097
    • Debski, B.1    Picciano, M.F.2    Milner, J.A.3
  • 43
    • 0002362857 scopus 로고
    • The role of enzymes in food flavors. Part I. Dairy products
    • B.K. Dwivedi The role of enzymes in food flavors. Part I. Dairy products CRC Critical Reviews in Food Technology 3 1973 457 478
    • (1973) CRC Critical Reviews in Food Technology , vol.3 , pp. 457-478
    • Dwivedi, B.K.1
  • 44
    • 84963986336 scopus 로고
    • Fluorometric analysis of alkaline phosphatase inactivation correlated to Salmonella and Listeria inactivation
    • K.F. Eckner Fluorometric analysis of alkaline phosphatase inactivation correlated to Salmonella and Listeria inactivation Journal of Food Protection 55 1992 960 963
    • (1992) Journal of Food Protection , vol.55 , pp. 960-963
    • Eckner, K.F.1
  • 46
    • 0016960211 scopus 로고
    • Relationship between composition and stability of bovine milk lysozome
    • R.R. Eitenmiller, B.A. Friend, and K.M. Shahani Relationship between composition and stability of bovine milk lysozome Journal of Dairy Science 59 1976 834 839
    • (1976) Journal of Dairy Science , vol.59 , pp. 834-839
    • Eitenmiller, R.R.1    Friend, B.A.2    Shahani, K.M.3
  • 48
    • 0016418267 scopus 로고
    • Influence of mastitis on properties of milk. XI. Fat globule membrane
    • R.W. Erwin, and H.E. Randolph Influence of mastitis on properties of milk. XI. Fat globule membrane Journal of Dairy Science 58 1975 9 12
    • (1975) Journal of Dairy Science , vol.58 , pp. 9-12
    • Erwin, R.W.1    Randolph, H.E.2
  • 49
    • 0006431593 scopus 로고    scopus 로고
    • Indigenous enzymes in milk; Other enzymes
    • P.F. Fox P.L.H. McSweeney 3rd ed. Kluwer Academic-Plenum Publishers New York, USA
    • N.Y. Farkye Indigenous enzymes in milk; other enzymes P.F. Fox P.L.H. McSweeney Advanced dairy chemistry, volume 1, proteins 3rd ed. 2003 Kluwer Academic-Plenum Publishers New York, USA 571 603
    • (2003) Advanced Dairy Chemistry, Volume 1, Proteins , pp. 571-603
    • Farkye, N.Y.1
  • 50
  • 51
    • 84906905450 scopus 로고
    • Lysozyme. a bacteriolytic ferment found normally in tissues and secretions
    • A. Fleming Lysozyme. A bacteriolytic ferment found normally in tissues and secretions The Lancet 1929 217 220
    • (1929) The Lancet , pp. 217-220
    • Fleming, A.1
  • 55
    • 0027145742 scopus 로고
    • Exogenous enzymes in dairy technology
    • P.F. Fox Exogenous enzymes in dairy technology Journal of Food Biochemistry 17 1993 173 199
    • (1993) Journal of Food Biochemistry , vol.17 , pp. 173-199
    • Fox, P.F.1
  • 56
    • 10044235534 scopus 로고    scopus 로고
    • Significance of indigenous enzymes in milk and dairy products
    • J.R. Whitaker A.G.J. Voragen D.W.S. Wong Marcel Dekker New York, USA
    • P.F. Fox Significance of indigenous enzymes in milk and dairy products J.R. Whitaker A.G.J. Voragen D.W.S. Wong Handbook of food enzymology 2003 Marcel Dekker New York, USA 255 277
    • (2003) Handbook of Food Enzymology , pp. 255-277
    • Fox, P.F.1
  • 57
    • 0000796762 scopus 로고
    • Exogenous enzymes in dairy technology
    • P.F. Fox Elsevier London, UK
    • P.F. Fox, and M.B. Grufferty Exogenous enzymes in dairy technology P.F. Fox Food enzymology 1991 Elsevier London, UK 219 269
    • (1991) Food Enzymology , pp. 219-269
    • Fox, P.F.1    Grufferty, M.B.2
  • 58
    • 33645393430 scopus 로고    scopus 로고
    • Indigenous enzymes in milk: Overview and historical aspects - Part 1
    • doi:10.1016/j.idairyj.2005.09.013
    • Fox, P. F., & Kelly, A. L. (2006). Indigenous enzymes in milk: Overview and historical aspects - part 1. International Dairy Journal, this issue, doi:10.1016/j.idairyj.2005.09.013.
    • (2006) International Dairy Journal , Issue.THIS ISSUE
    • Fox, P.F.1    Kelly, A.L.2
  • 59
    • 33645412457 scopus 로고
    • Indigenous enzymes of bovine milk
    • G.G. Birch N. Blakeborough K.J. Parker Applied Science Publishers London, UK
    • P.F. Fox, and P.A. Morrissey Indigenous enzymes of bovine milk G.G. Birch N. Blakeborough K.J. Parker Enzymes and food processing 1981 Applied Science Publishers London, UK 213 238
    • (1981) Enzymes and Food Processing , pp. 213-238
    • Fox, P.F.1    Morrissey, P.A.2
  • 64
    • 84987378200 scopus 로고
    • Role of the lysine, tyrosine and tryptophan residues in the activity of milk lysozymes
    • B.A. Friend, R.R. Eitenmiller, and K.M. Shahani Role of the lysine, tyrosine and tryptophan residues in the activity of milk lysozymes Journal of Food Science 40 1975 833 836
    • (1975) Journal of Food Science , vol.40 , pp. 833-836
    • Friend, B.A.1    Eitenmiller, R.R.2    Shahani, K.M.3
  • 65
    • 0014095853 scopus 로고
    • The isolation of lipoprotein particles from bovine milk by a gel-filtration procedure
    • D.B. Gammack, and B.B. Gupta The isolation of lipoprotein particles from bovine milk by a gel-filtration procedure Biochemical Journal 103 1967 72P [abstr.]
    • (1967) Biochemical Journal , vol.103
    • Gammack, D.B.1    Gupta, B.B.2
  • 67
    • 84914413046 scopus 로고
    • Phosphorus compounds in milk. V. the phosphorus partition in milk with preliminary observations on milk phosphatase
    • W.R. Graham, and H.D. Kay Phosphorus compounds in milk. V. The phosphorus partition in milk with preliminary observations on milk phosphatase Journal of Dairy Research 5 1933 54 62
    • (1933) Journal of Dairy Research , vol.5 , pp. 54-62
    • Graham, W.R.1    Kay, H.D.2
  • 68
    • 0001588557 scopus 로고
    • Use of milk enzymes as indices of heat treatment
    • M.W. Griffiths Use of milk enzymes as indices of heat treatment Journal of Food Protection 49 1986 696 705
    • (1986) Journal of Food Protection , vol.49 , pp. 696-705
    • Griffiths, M.W.1
  • 70
    • 33645408657 scopus 로고
    • Level and distribution of ribonuclease in milk from different species
    • N. Gupta, and M.P. Mathur Level and distribution of ribonuclease in milk from different species Indian Journal of Dairy Science 42 1989 547 549
    • (1989) Indian Journal of Dairy Science , vol.42 , pp. 547-549
    • Gupta, N.1    Mathur, M.P.2
  • 71
    • 0008013982 scopus 로고
    • Variations in alkaline phosphatase activity of milk
    • W. Haab, and L.M. Smith Variations in alkaline phosphatase activity of milk Journal of Dairy Science 39 1956 1644 1650
    • (1956) Journal of Dairy Science , vol.39 , pp. 1644-1650
    • Haab, W.1    Smith, L.M.2
  • 72
    • 0018332270 scopus 로고
    • Alkaline phosphatase from human milk. Comparison with isoenzymes from placenta and liver
    • T.A. Hamilton, S.Z. Gornicki, and H.H. Sussman Alkaline phosphatase from human milk. Comparison with isoenzymes from placenta and liver Biochemical Journal 177 1979 197 201
    • (1979) Biochemical Journal , vol.177 , pp. 197-201
    • Hamilton, T.A.1    Gornicki, S.Z.2    Sussman, H.H.3
  • 73
    • 33645382455 scopus 로고    scopus 로고
    • Superoxide dismutase
    • J.R. Whitaker A.G.J. Voragen D.W.S. Wong Marcel Dekker New York, USA
    • H. Hara, T. Adachi, and K. Hirano Superoxide dismutase J.R. Whitaker A.G.J. Voragen D.W.S. Wong Handbook of food enzymology 2003 Marcel Dekker New York, USA 503 508
    • (2003) Handbook of Food Enzymology , pp. 503-508
    • Hara, H.1    Adachi, T.2    Hirano, K.3
  • 74
    • 0025021039 scopus 로고
    • The human alkaline phosphatases: What we know and what we don't know
    • H. Harris The human alkaline phosphatases: What we know and what we don't know Clinica Chimica Acta 186 1989 133 150
    • (1989) Clinica Chimica Acta , vol.186 , pp. 133-150
    • Harris, H.1
  • 76
    • 0019034154 scopus 로고
    • Occurrence and consequences of superoxide dismutase in milk: A review
    • C.L. Hicks Occurrence and consequences of superoxide dismutase in milk: A review Journal of Dairy Science 63 1980 1199 1204
    • (1980) Journal of Dairy Science , vol.63 , pp. 1199-1204
    • Hicks, C.L.1
  • 78
    • 0000709182 scopus 로고
    • Variation of superoxide dismutase of bovine milk
    • J. Holbrook, and C.L. Hicks Variation of superoxide dismutase of bovine milk Journal of Dairy Science 61 1978 1072 1077
    • (1978) Journal of Dairy Science , vol.61 , pp. 1072-1077
    • Holbrook, J.1    Hicks, C.L.2
  • 79
    • 77956895467 scopus 로고
    • Aldolases
    • P. Boyer 3rd ed. Academic Press New York, USA
    • B. Horecker, O. Tsolas, and C. Lai Aldolases P. Boyer The enzymes, volume 7 3rd ed. 1972 Academic Press New York, USA 213 230
    • (1972) The Enzymes, Volume 7 , pp. 213-230
    • Horecker, B.1    Tsolas, O.2    Lai, C.3
  • 80
    • 0025997931 scopus 로고
    • Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase
    • M.F. Hoylaerts, and J.L. Millan Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase European Journal of Biochemistry 202 1991 605 616
    • (1991) European Journal of Biochemistry , vol.202 , pp. 605-616
    • Hoylaerts, M.F.1    Millan, J.L.2
  • 81
    • 33645269424 scopus 로고
    • Sodium phenolphthalein phosphate as a substrate for phosphatase tests
    • C. Huggins, and P. Talalay Sodium phenolphthalein phosphate as a substrate for phosphatase tests Journal of Biological Chemistry 159 1948 399 410
    • (1948) Journal of Biological Chemistry , vol.159 , pp. 399-410
    • Huggins, C.1    Talalay, P.2
  • 82
    • 0027252943 scopus 로고
    • The primary structures and properties of non-stomach lysozymes of sheep and cow, and implications for functional divergence of lysozyme
    • Y. Ito, H. Yamada, M. Nakamura, A. Yoshikawa, T. Ueda, and T. Imoto The primary structures and properties of non-stomach lysozymes of sheep and cow, and implications for functional divergence of lysozyme European Journal of Biochemistry 213 1993 649 658
    • (1993) European Journal of Biochemistry , vol.213 , pp. 649-658
    • Ito, Y.1    Yamada, H.2    Nakamura, M.3    Yoshikawa, A.4    Ueda, T.5    Imoto, T.6
  • 83
    • 0016798404 scopus 로고
    • Isolation and characterization of sulfhydryl oxidase from bovine milk
    • V.G. Janolino, and H.E. Swaisgood Isolation and characterization of sulfhydryl oxidase from bovine milk Journal of Biological Chemistry 250 1975 2532 2538
    • (1975) Journal of Biological Chemistry , vol.250 , pp. 2532-2538
    • Janolino, V.G.1    Swaisgood, H.E.2
  • 84
    • 0642291317 scopus 로고
    • Effect of support pore size on activity of immobilized sulfhydryl oxidase
    • V.G. Janolino, and H.E. Swaisgood Effect of support pore size on activity of immobilized sulfhydryl oxidase Journal of Dairy Science 61 1978 393 399
    • (1978) Journal of Dairy Science , vol.61 , pp. 393-399
    • Janolino, V.G.1    Swaisgood, H.E.2
  • 85
    • 0015196612 scopus 로고
    • Purification of lysozymes by retention on Bio Gel GM 30
    • J. Jauregui-Adell Purification of lysozymes by retention on Bio Gel GM 30 Biochemie 53 1971 1167 1173
    • (1971) Biochemie , vol.53 , pp. 1167-1173
    • Jauregui-Adell, J.1
  • 86
    • 0016517114 scopus 로고
    • Heat stability and reactivation of mare milk lysozyme
    • J. Jauregui-Adell Heat stability and reactivation of mare milk lysozyme Journal of Dairy Science 58 1975 835 838
    • (1975) Journal of Dairy Science , vol.58 , pp. 835-838
    • Jauregui-Adell, J.1
  • 88
  • 89
    • 0014052921 scopus 로고
    • Human tear and human milk lysozymes
    • J. Jolles, and P. Jolles Human tear and human milk lysozymes Biochemistry 6 1967 411 417
    • (1967) Biochemistry , vol.6 , pp. 411-417
    • Jolles, J.1    Jolles, P.2
  • 90
    • 0010742387 scopus 로고
    • Comparison between human and bird lypozymes: Note concerning the previously observed deletion
    • J. Jolles, and P. Jolles Comparison between human and bird lypozymes: Note concerning the previously observed deletion FEBS Letters 22 1972 31 33
    • (1972) FEBS Letters , vol.22 , pp. 31-33
    • Jolles, J.1    Jolles, P.2
  • 91
    • 0010539913 scopus 로고
    • Lysozyme from human milk
    • P. Jolles, and J. Jolles Lysozyme from human milk Nature 192 1961 1187 1188
    • (1961) Nature , vol.192 , pp. 1187-1188
    • Jolles, P.1    Jolles, J.2
  • 92
    • 1542390011 scopus 로고
    • Determination and interpretation of alkaline phosphatase activity in experimental and commercial butters
    • R. Karmas, and D.H. Kleyn Determination and interpretation of alkaline phosphatase activity in experimental and commercial butters Journal of Dairy Science 73 1990 584 589
    • (1990) Journal of Dairy Science , vol.73 , pp. 584-589
    • Karmas, R.1    Kleyn, D.H.2
  • 93
    • 0014192404 scopus 로고
    • Tertiary structure of ribonuclease
    • G. Kartha, J. Bello, and D. Harker Tertiary structure of ribonuclease Nature 213 1967 862 865
    • (1967) Nature , vol.213 , pp. 862-865
    • Kartha, G.1    Bello, J.2    Harker, D.3
  • 94
    • 33645408177 scopus 로고    scopus 로고
    • Lysozyme
    • J.R. Whitaker A.G.J. Voragen D.W.S. Wong Marcel Dekker New York, USA
    • A. Kato Lysozyme J.R. Whitaker A.G.J. Voragen D.W.S. Wong Handbook of food enzymology 2003 Marcel Dekker New York, USA 971 978
    • (2003) Handbook of Food Enzymology , pp. 971-978
    • Kato, A.1
  • 95
    • 33645380908 scopus 로고
    • Phosphorus compounds in milk. VI. the effect of heat on milk phosphatase. a simple method for distinguishing raw from pasteurised milk, and raw cream from pasteurised cream and butter from raw cream from that made from pasteurised cream
    • H.D. Kay, and W.R. Graham Phosphorus compounds in milk. VI. The effect of heat on milk phosphatase. A simple method for distinguishing raw from pasteurised milk, and raw cream from pasteurised cream and butter from raw cream from that made from pasteurised cream Journal of Dairy Research 5 1933 63 74
    • (1933) Journal of Dairy Research , vol.5 , pp. 63-74
    • Kay, H.D.1    Graham, W.R.2
  • 96
    • 0008014579 scopus 로고
    • The phosphatase test for pasteurised milk
    • H.D. Kay, and W.R. Graham The phosphatase test for pasteurised milk Journal of Dairy Research 6 1935 191 203
    • (1935) Journal of Dairy Research , vol.6 , pp. 191-203
    • Kay, H.D.1    Graham, W.R.2
  • 98
    • 0002310126 scopus 로고
    • Intracellular origin of milk lipid globules and the nature and structure of the milk fat globule membrane
    • P.F. Fox 2nd ed. Chapman & Hall London, UK
    • T.W. Keenan, and D.F. Dylewski Intracellular origin of milk lipid globules and the nature and structure of the milk fat globule membrane P.F. Fox Advanced dairy chemistry 2nd ed. 1995 Chapman & Hall London, UK 89 130
    • (1995) Advanced Dairy Chemistry , pp. 89-130
    • Keenan, T.W.1    Dylewski, D.F.2
  • 99
    • 84885703019 scopus 로고    scopus 로고
    • Intracellular origin of milk fat globules and the nature of the milk fat globule membrane
    • P.F. Fox P.L.H. McSweeney 3rd ed. Kluwer Acaemic-Plenum Publishers New York, USA
    • T.W. Keenan, and I.H. Mather Intracellular origin of milk fat globules and the nature of the milk fat globule membrane P.F. Fox P.L.H. McSweeney Advanced dairy chemistry, volume 2 - Lipids 3rd ed. 2006 Kluwer Acaemic-Plenum Publishers New York, USA 137 171
    • (2006) Advanced Dairy Chemistry, Volume 2 - Lipids , pp. 137-171
    • Keenan, T.W.1    Mather, I.H.2
  • 100
    • 0001934484 scopus 로고
    • Physical equilibria, lipid phase
    • N.P. Wong R. Jenness M. Kenney E.H. Marth 3rd ed. Van Norstrand Reinhold New York, USA
    • T.W. Keenan, I.H. Mather, and D.F. Dylewski Physical equilibria, lipid phase N.P. Wong R. Jenness M. Kenney E.H. Marth Fundamentals of dairy chemistry 3rd ed. 1988 Van Norstrand Reinhold New York, USA 511 582
    • (1988) Fundamentals of Dairy Chemistry , pp. 511-582
    • Keenan, T.W.1    Mather, I.H.2    Dylewski, D.F.3
  • 101
    • 33645396800 scopus 로고
    • γ-Glutamyl transferase (γ-glutamyl transpeptidase)
    • A.J. Barrett North-Holland Amsterdam, The Netherlands
    • A.J. Kenny γ-Glutamyl transferase (γ-glutamyl transpeptidase) A.J. Barrett Proteinases in mammalian cells and tissues 1977 North-Holland Amsterdam, The Netherlands 410 417
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 410-417
    • Kenny, A.J.1
  • 102
    • 10544228446 scopus 로고
    • An enzyme in milk which oxidizes sulphydryl groups. I. Isolation and characterization of the enzyme
    • F. Kiermeier, and E. Petz An enzyme in milk which oxidizes sulphydryl groups. I. Isolation and characterization of the enzyme Zeitschrift fur Lebensmittel-Untersuchung und -Forschung 132 1967 342 352
    • (1967) Zeitschrift fur Lebensmittel-Untersuchung und -Forschung , vol.132 , pp. 342-352
    • Kiermeier, F.1    Petz, E.2
  • 103
    • 0025181742 scopus 로고
    • Structure of alkaline phosphatases
    • E.E. Kim, and H.M. Wyckoff Structure of alkaline phosphatases Clinica Chemica Acta 186 1990 175 188
    • (1990) Clinica Chemica Acta , vol.186 , pp. 175-188
    • Kim, E.E.1    Wyckoff, H.M.2
  • 104
    • 0016965879 scopus 로고
    • Enzymatic methods for estimation of the somatic cell count in bovine milk. I. Development of assay techniques and a study of their usefulness in evaluating the somatic cell content of milk
    • B.J. Kitchen Enzymatic methods for estimation of the somatic cell count in bovine milk. I. Development of assay techniques and a study of their usefulness in evaluating the somatic cell content of milk Journal of Dairy Research 43 1976 251 258
    • (1976) Journal of Dairy Research , vol.43 , pp. 251-258
    • Kitchen, B.J.1
  • 105
    • 0019525766 scopus 로고
    • Review of the progress of dairy science, bovine mastitis: Compositional changes and related diagnostic tests
    • B.J. Kitchen Review of the progress of dairy science, bovine mastitis: Compositional changes and related diagnostic tests Journal of Dairy Research 48 1981 167 188
    • (1981) Journal of Dairy Research , vol.48 , pp. 167-188
    • Kitchen, B.J.1
  • 107
    • 0022246438 scopus 로고
    • Purification and properties of bovine mammary gland N-acetyl-β-d- glucosaminidase
    • B.J. Kitchen, and C.J. Masters Purification and properties of bovine mammary gland N-acetyl-β-d-glucosaminidase Biochimica et Biophysica Acta 831 1985 125 132
    • (1985) Biochimica et Biophysica Acta , vol.831 , pp. 125-132
    • Kitchen, B.J.1    Masters, C.J.2
  • 108
    • 0017010401 scopus 로고
    • Enzymatic methods for the estimation of the somatic cell count in bovine milk. II. N-Acetyl-β-d-glucosaminidase test for routine estimation of the somatic cell count in milk
    • B.J. Kitchen, and G. Midleton Enzymatic methods for the estimation of the somatic cell count in bovine milk. II. N-Acetyl-β-d-glucosaminidase test for routine estimation of the somatic cell count in milk Journal of Dairy Research 43 1976 491 494
    • (1976) Journal of Dairy Research , vol.43 , pp. 491-494
    • Kitchen, B.J.1    Midleton, G.2
  • 109
    • 0017931837 scopus 로고
    • Bovine milk N-acetyl-β-d-glucosaminidase and its significance in the detection of abnormal udder secretions
    • B.J. Kitchen, G. Mitleton, and M. Salmon Bovine milk N-acetyl-β-d- glucosaminidase and its significance in the detection of abnormal udder secretions Journal of Dairy Research 45 1978 15 20
    • (1978) Journal of Dairy Research , vol.45 , pp. 15-20
    • Kitchen, B.J.1    Mitleton, G.2    Salmon, M.3
  • 111
    • 0018013719 scopus 로고
    • Rapid screening method for alkaline phosphatase activity in cheese: Collaborative study
    • D.H. Kleyn Rapid screening method for alkaline phosphatase activity in cheese: Collaborative study Journal of the Association of Official Analytical Chemists 61 1978 1035 1037
    • (1978) Journal of the Association of Official Analytical Chemists , vol.61 , pp. 1035-1037
    • Kleyn, D.H.1
  • 112
    • 33645409929 scopus 로고
    • Dialysis phosphatase method for milk and all dairy products
    • F.V. Kosikowski Dialysis phosphatase method for milk and all dairy products Journal of Dairy Science 47 1964 748 753
    • (1964) Journal of Dairy Science , vol.47 , pp. 748-753
    • Kosikowski, F.V.1
  • 113
    • 33645416414 scopus 로고
    • Interpretation of the milk alkaline phosphatase reactivation process
    • G.C. Kresheck, and W.J. Harper Interpretation of the milk alkaline phosphatase reactivation process Milchwissenschaft 22 1967 72 75
    • (1967) Milchwissenschaft , vol.22 , pp. 72-75
    • Kresheck, G.C.1    Harper, W.J.2
  • 116
    • 0014169272 scopus 로고
    • Isolation and purification of 2 alkaline phosphatase fractions from cows' milk
    • G. Le Franc, and K. Han Isolation and purification of 2 alkaline phosphatase fractions from cows' milk Annales Pasteur Institut, Lille 18 1967 185 196
    • (1967) Annales Pasteur Institut, Lille , vol.18 , pp. 185-196
    • Le Franc, G.1    Han, K.2
  • 117
    • 0024747798 scopus 로고
    • Subcellular and ultrastructural localization of alkaline phosphatase in lactating rat mammary gland
    • C.T. Leung, B.E. Maleeff, and H.M. Farrell Jr. Subcellular and ultrastructural localization of alkaline phosphatase in lactating rat mammary gland Journal of Dairy Science 72 1989 2495 2509
    • (1989) Journal of Dairy Science , vol.72 , pp. 2495-2509
    • Leung, C.T.1    Maleeff, B.E.2    Farrell Jr., H.M.3
  • 118
    • 0040215908 scopus 로고
    • Biochemical study of some aspects of milk alkaline phosphatase reactivation
    • G. Linden Biochemical study of some aspects of milk alkaline phosphatase reactivation Milchwissenschaft 34 1979 329 332
    • (1979) Milchwissenschaft , vol.34 , pp. 329-332
    • Linden, G.1
  • 119
    • 0017280510 scopus 로고
    • Phosphatase alkaline du lait de vache. II. Structure sous-unitaire, nature metalloproteique et parameters cinetiques
    • G. Linden, and C. Alais Phosphatase alkaline du lait de vache. II. Structure sous-unitaire, nature metalloproteique et parameters cinetiques Biochimica et Biophysica Acta 429 1976 205 213
    • (1976) Biochimica et Biophysica Acta , vol.429 , pp. 205-213
    • Linden, G.1    Alais, C.2
  • 120
    • 0017864565 scopus 로고
    • Alkaline phosphatase in human, cow and sheep milk: Molecular and catalytic properties and metal ion action
    • G. Linden, and C. Alais Alkaline phosphatase in human, cow and sheep milk: Molecular and catalytic properties and metal ion action Annales de Biologie Animale Biochemie Biophysique 18 1978 749 758
    • (1978) Annales de Biologie Animale Biochemie Biophysique , vol.18 , pp. 749-758
    • Linden, G.1    Alais, C.2
  • 121
  • 122
    • 33645417336 scopus 로고    scopus 로고
    • Glutathione peroxidase
    • J.R. Whitaker A.G.J. Voragen D.W.S. Wong Marcel Dekker New York, USA
    • J.-Q. Liu, and G.-M. Luo Glutathione peroxidase J.R. Whitaker A.G.J. Voragen D.W.S. Wong Handbook of food enzymology 2003 Marcel Dekker New York, USA 413 424
    • (2003) Handbook of Food Enzymology , pp. 413-424
    • Liu, J.-Q.1    Luo, G.-M.2
  • 123
    • 0542414813 scopus 로고
    • The reactivation of milk alkaline phosphatase after heat treatment
    • R.L.T. Lyster, and R. Aschaffenburg The reactivation of milk alkaline phosphatase after heat treatment Journal of Dairy Research 29 1962 21 34
    • (1962) Journal of Dairy Research , vol.29 , pp. 21-34
    • Lyster, R.L.T.1    Aschaffenburg, R.2
  • 126
    • 0003570017 scopus 로고
    • Superoxidase dismutase: A history
    • A.M. Michelson J.M. McCord I. Fridovich Academic Press London, UK
    • J.M. McCord, and I. Fridovich Superoxidase dismutase: A history A.M. Michelson J.M. McCord I. Fridovich Superoxide and superoxide dismutases 1977 Academic Press London, UK 1 10
    • (1977) Superoxide and Superoxide Dismutases , pp. 1-10
    • McCord, J.M.1    Fridovich, I.2
  • 127
    • 0016317509 scopus 로고
    • RNase inhibition of reverse transcriptase activity in human milk
    • J.J. McCormick, L.J. Larson, and M.A. Rich RNase inhibition of reverse transcriptase activity in human milk Nature 251 1974 737 740
    • (1974) Nature , vol.251 , pp. 737-740
    • McCormick, J.J.1    Larson, L.J.2    Rich, M.A.3
  • 128
    • 0030291102 scopus 로고    scopus 로고
    • Influence of ice-cream mix components on the thermal stability of bovine γ-glutamyl transpeptidase and Listeria innocua
    • R.C. McKellar Influence of ice-cream mix components on the thermal stability of bovine γ-glutamyl transpeptidase and Listeria innocua International Dairy Journal 6 1996 1181 1189
    • (1996) International Dairy Journal , vol.6 , pp. 1181-1189
    • McKellar, R.C.1
  • 129
    • 0000808810 scopus 로고
    • Gamma-glutamyl transpeptidase in milk and butter as an indicator of heat treatment
    • R.C. McKellar, D.B. Emmons, and J. Farber Gamma-glutamyl transpeptidase in milk and butter as an indicator of heat treatment International Dairy Journal 1 1991 241 251
    • (1991) International Dairy Journal , vol.1 , pp. 241-251
    • McKellar, R.C.1    Emmons, D.B.2    Farber, J.3
  • 130
    • 0030097918 scopus 로고    scopus 로고
    • Predictive modeling of lactoperoxidase and γ-glutamyl transpeptidase inactivation in a high-temperature short-time pasteurizer
    • R.C. McKellar, S. Liou, and H.W. Modler Predictive modeling of lactoperoxidase and γ-glutamyl transpeptidase inactivation in a high-temperature short-time pasteurizer International Dairy Journal 6 1996 295 301
    • (1996) International Dairy Journal , vol.6 , pp. 295-301
    • McKellar, R.C.1    Liou, S.2    Modler, H.W.3
  • 132
    • 0018748105 scopus 로고
    • Comparison of human alkaline phosphatase isoenzymes. Structural evident for three protein classes
    • M.J. McKenna, T.A. Hamilton, and H.H. Sussman Comparison of human alkaline phosphatase isoenzymes. Structural evident for three protein classes Biochemical Journal 181 1979 67 73
    • (1979) Biochemical Journal , vol.181 , pp. 67-73
    • McKenna, M.J.1    Hamilton, T.A.2    Sussman, H.H.3
  • 133
    • 0021918936 scopus 로고
    • The amino acid sequence of equine milk lysozyme
    • H.A. McKenzie, and D.C. Shaw The amino acid sequence of equine milk lysozyme Biochemistry International 10 1985 23 31
    • (1985) Biochemistry International , vol.10 , pp. 23-31
    • McKenzie, H.A.1    Shaw, D.C.2
  • 134
    • 0025811817 scopus 로고
    • Lysozyme and α-lactalbumin, structure, function, and interrelationships
    • H.A. McKenzie, and F.H. White Jr. Lysozyme and α-lactalbumin, structure, function, and interrelationships Advanced Protein Chemistry 41 1991 173 315
    • (1991) Advanced Protein Chemistry , vol.41 , pp. 173-315
    • McKenzie, H.A.1    White Jr., F.H.2
  • 135
    • 0015915903 scopus 로고
    • On the enzymology of amino acid transport
    • A. Meister On the enzymology of amino acid transport Science 180 1973 33 39
    • (1973) Science , vol.180 , pp. 33-39
    • Meister, A.1
  • 136
    • 0014284844 scopus 로고
    • β-N-acetylglucosaminase in bovine milk
    • A. Mellors β-N-acetylglucosaminase in bovine milk Canadian Journal of Biochemistry 46 1968 451 455
    • (1968) Canadian Journal of Biochemistry , vol.46 , pp. 451-455
    • Mellors, A.1
  • 137
    • 0023408856 scopus 로고
    • Ribonuclease activity and isoenzymes in raw and processed cows' milk and infant formulas
    • D.H. Meyer, A.S. Kunin, J. Maddalena, and W.L. Meyer Ribonuclease activity and isoenzymes in raw and processed cows' milk and infant formulas Journal of Dairy Science 70 1987 1797 1803
    • (1987) Journal of Dairy Science , vol.70 , pp. 1797-1803
    • Meyer, D.H.1    Kunin, A.S.2    Maddalena, J.3    Meyer, W.L.4
  • 138
    • 33645387821 scopus 로고
    • Ribonuclease II isoenzymes in milk: Their possible immunologic role and use as diagnostic tools
    • W.L. Meyer, D.H. Meyer, A.S. Kunin, E.L. Capeless, K.R. Simmons, and J.W. Pankey Ribonuclease II isoenzymes in milk: Their possible immunologic role and use as diagnostic tools Journal of Dairy Science 70 Suppl. 1 1987 266 [abstr.]
    • (1987) Journal of Dairy Science , vol.70 , Issue.1 SUPPL. , pp. 266
    • Meyer, W.L.1    Meyer, D.H.2    Kunin, A.S.3    Capeless, E.L.4    Simmons, K.R.5    Pankey, J.W.6
  • 139
    • 0027437455 scopus 로고
    • Phase 1 human clinical trial of onconase (P-30 protein) administered intravenously on a weekly schedule in cancer patients with solid tumours
    • S.M. Mikulski, A.M. Grosmann, P.W. Carter, K. Shogen, and J.J. Costanzi Phase 1 human clinical trial of onconase (P-30 protein) administered intravenously on a weekly schedule in cancer patients with solid tumours International Journal of Oncology 3 1993 57 64
    • (1993) International Journal of Oncology , vol.3 , pp. 57-64
    • Mikulski, S.M.1    Grosmann, A.M.2    Carter, P.W.3    Shogen, K.4    Costanzi, J.J.5
  • 140
    • 0039040625 scopus 로고
    • Separation and purification of enzymes associated with insoluble particles
    • R.K. Morton Separation and purification of enzymes associated with insoluble particles Nature 166 1950 1092 1095
    • (1950) Nature , vol.166 , pp. 1092-1095
    • Morton, R.K.1
  • 141
    • 33645383382 scopus 로고
    • Microsomal particles of normal cow's milk
    • R.K. Morton Microsomal particles of normal cow's milk Nature 171 1953 734 735
    • (1953) Nature , vol.171 , pp. 734-735
    • Morton, R.K.1
  • 142
    • 0040743986 scopus 로고
    • The lipoprotein particles of cow's milk
    • R.K. Morton The lipoprotein particles of cow's milk Biochemical Journal 57 1954 231 237
    • (1954) Biochemical Journal , vol.57 , pp. 231-237
    • Morton, R.K.1
  • 143
    • 0019989821 scopus 로고
    • Alkaline phosphatase isoenzymes
    • D.W. Moss Alkaline phosphatase isoenzymes Clinical Chemistry 28 1982 2007 2016
    • (1982) Clinical Chemistry , vol.28 , pp. 2007-2016
    • Moss, D.W.1
  • 144
    • 0027080073 scopus 로고
    • Perspectives in alkaline phosphatase research
    • D.W. Moss Perspectives in alkaline phosphatase research Clinical Chemistry 38 1992 2486 2492
    • (1992) Clinical Chemistry , vol.38 , pp. 2486-2492
    • Moss, D.W.1
  • 145
    • 15444368669 scopus 로고
    • The acid phosphatase of cow's milk
    • J.E.C. Mullen The acid phosphatase of cow's milk Journal of Dairy Research 17 1950 288 305
    • (1950) Journal of Dairy Research , vol.17 , pp. 288-305
    • Mullen, J.E.C.1
  • 146
    • 0017011342 scopus 로고
    • Reactivation of alkaline phosphatase in ultra high-temperature, short-time processed liquid milk products
    • G.K. Murthy, S. Cox, and L. Kaylor Reactivation of alkaline phosphatase in ultra high-temperature, short-time processed liquid milk products Journal of Dairy Science 59 1976 1699 1710
    • (1976) Journal of Dairy Science , vol.59 , pp. 1699-1710
    • Murthy, G.K.1    Cox, S.2    Kaylor, L.3
  • 147
    • 0018499957 scopus 로고
    • Rapid methods for differentiating reactivated from residual phosphatase in milk and cream: Collaborative study
    • G.K. Murthy, and J.T. Peeler Rapid methods for differentiating reactivated from residual phosphatase in milk and cream: Collaborative study Journal of the Association of Official Analytical Chemists 62 1979 822 827
    • (1979) Journal of the Association of Official Analytical Chemists , vol.62 , pp. 822-827
    • Murthy, G.K.1    Peeler, J.T.2
  • 148
    • 0013980707 scopus 로고
    • Automated test for milk phosphatase
    • J.E. O'Brien Automated test for milk phosphatase Journal of Dairy Science 49 1966 1482 1487
    • (1966) Journal of Dairy Science , vol.49 , pp. 1482-1487
    • O'Brien, J.E.1
  • 149
    • 0018369742 scopus 로고
    • Alkaline phosphatase from bovine mammary tissue: Purification and some molecular and catalytic properties
    • R.B. O'Keefe, and J.E. Kinsella Alkaline phosphatase from bovine mammary tissue: Purification and some molecular and catalytic properties International Journal of Biochemistry 10 1979 125 134
    • (1979) International Journal of Biochemistry , vol.10 , pp. 125-134
    • O'Keefe, R.B.1    Kinsella, J.E.2
  • 151
    • 85005586916 scopus 로고
    • Heat exchanger performance: γ-Glutamyl transpeptidase assay as a heat treatment indicator for dairy products
    • S.S. Patel, and R.A. Wilbey Heat exchanger performance: γ-Glutamyl transpeptidase assay as a heat treatment indicator for dairy products Journal of the Society of Dairy Technology 42 1989 79 80
    • (1989) Journal of the Society of Dairy Technology , vol.42 , pp. 79-80
    • Patel, S.S.1    Wilbey, R.A.2
  • 152
    • 0033744361 scopus 로고    scopus 로고
    • A sensitive HPLC method to detect hen's egg white lysozome in milk and dairy products
    • L. Pellegrino, and A. Tirelli A sensitive HPLC method to detect hen's egg white lysozome in milk and dairy products International Dairy Journal 10 2000 435 442
    • (2000) International Dairy Journal , vol.10 , pp. 435-442
    • Pellegrino, L.1    Tirelli, A.2
  • 155
    • 0036698142 scopus 로고    scopus 로고
    • Purification, characterization, antibacterial activity and N-terminal sequencing of buffalo-milk lysozyme
    • S. Pryadarshini, and V.K. Kansal Purification, characterization, antibacterial activity and N-terminal sequencing of buffalo-milk lysozyme Journal of Dairy Research 69 2002 419 431
    • (2002) Journal of Dairy Research , vol.69 , pp. 419-431
    • Pryadarshini, S.1    Kansal, V.K.2
  • 156
    • 0242404305 scopus 로고    scopus 로고
    • Biochemical characterization of buffalo (Bubalus bubalis) milk lysozyme
    • S. Pryadarshini, and V.K. Kansal Biochemical characterization of buffalo (Bubalus bubalis) milk lysozyme Journal of Dairy Research 70 2003 467 471
    • (2003) Journal of Dairy Research , vol.70 , pp. 467-471
    • Pryadarshini, S.1    Kansal, V.K.2
  • 157
    • 0031266680 scopus 로고    scopus 로고
    • Accuracy of methods using somatic cell count and N-acetyl-β-d- glucosaminidase activity in milk to assess the bacteriological cure of bovine clinical mastitis
    • S. Pyörälä, and E. Pyörälä Accuracy of methods using somatic cell count and N-acetyl-β-d-glucosaminidase activity in milk to assess the bacteriological cure of bovine clinical mastitis Journal of Dairy Science 80 1997 2820 2825
    • (1997) Journal of Dairy Science , vol.80 , pp. 2820-2825
    • Pyörälä, S.1    Pyörälä, E.2
  • 158
    • 0027467427 scopus 로고
    • Purification of high molecular weight ribonuclease from human milk
    • H. Ramaswamy, C.V.B. Swamy, and R.M. Das Purification of high molecular weight ribonuclease from human milk Journal of Biological Chemistry 268 1993 4181 4187
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 4181-4187
    • Ramaswamy, H.1    Swamy, C.V.B.2    Das, R.M.3
  • 159
    • 2942719013 scopus 로고    scopus 로고
    • Use of a fluorometric test for bovine alkaline phosphatase to demonstrate underpasteurisation of skimmed milk and cream
    • A.M. Rampling, M.H. Greenwood, and G.E.N. Davies Use of a fluorometric test for bovine alkaline phosphatase to demonstrate underpasteurisation of skimmed milk and cream International Dairy Journal 14 2004 691 695
    • (2004) International Dairy Journal , vol.14 , pp. 691-695
    • Rampling, A.M.1    Greenwood, M.H.2    Davies, G.E.N.3
  • 160
    • 33645382454 scopus 로고
    • Application of an automated procedure to the milk phosphatase test
    • R.C. Reynolds, and W.J.P. Telford Application of an automated procedure to the milk phosphatase test Journal of Food Technology 30 1967 21 25
    • (1967) Journal of Food Technology , vol.30 , pp. 21-25
    • Reynolds, R.C.1    Telford, W.J.P.2
  • 161
    • 0000869476 scopus 로고
    • Fluorometric analysis of alkaline phosphatase in fluid dairy products
    • Rocco, R. M. (1990). Fluorometric analysis of alkaline phosphatase in fluid dairy products. Journal of Food Protection, 53, 588-591, 630-631.
    • (1990) Journal of Food Protection , vol.53 , pp. 588-591
    • Rocco, R.M.1
  • 162
    • 0006396286 scopus 로고
    • Changes in ribonuclease concentration during lactation in cows' colostrum and milk
    • M. Roman, L. Sanchez, and M. Calvo Changes in ribonuclease concentration during lactation in cows' colostrum and milk Netherlands Milk and Dairy Journal 44 1990 207 212
    • (1990) Netherlands Milk and Dairy Journal , vol.44 , pp. 207-212
    • Roman, M.1    Sanchez, L.2    Calvo, M.3
  • 164
    • 85010252383 scopus 로고
    • Modification of the phosphatase test as applied to Cheddar cheese and application of the test to fluid milk
    • G.P. Sanders, and O.S. Sager Modification of the phosphatase test as applied to Cheddar cheese and application of the test to fluid milk Journal of Dairy Science 29 1946 737 749
    • (1946) Journal of Dairy Science , vol.29 , pp. 737-749
    • Sanders, G.P.1    Sager, O.S.2
  • 165
    • 0008014758 scopus 로고
    • A rapid phosphomonoesterase test for control of dairy pasteurization
    • H. Scharer A rapid phosphomonoesterase test for control of dairy pasteurization Journal of Dairy Science 21 1938 21 34
    • (1938) Journal of Dairy Science , vol.21 , pp. 21-34
    • Scharer, H.1
  • 166
    • 78651114304 scopus 로고
    • Tissue fractionation studies. 15. Intracellular distribution and properties of β-N-acetylglucosaminidase and β-galactosidase in rat liver
    • O.Z. Sellinger, H. Beaufay, P. Jacques, A. Doyen, and C. de Duve Tissue fractionation studies. 15. Intracellular distribution and properties of β-N-acetylglucosaminidase and β-galactosidase in rat liver Biochemical Journal 74 1960 450 456
    • (1960) Biochemical Journal , vol.74 , pp. 450-456
    • Sellinger, O.Z.1    Beaufay, H.2    Jacques, P.3    Doyen, A.4    De Duve, C.5
  • 167
    • 11144343635 scopus 로고    scopus 로고
    • Rapid and highly sensitive electrochemical determination of alkaline phosphatase using a composite tyrosinase biosensor
    • B. Serra, M.D. Morales, A.J. Reviejo, E.H. Hall, and J.M. Pingarron Rapid and highly sensitive electrochemical determination of alkaline phosphatase using a composite tyrosinase biosensor Analytical Biochemistry 336 2005 289 294
    • (2005) Analytical Biochemistry , vol.336 , pp. 289-294
    • Serra, B.1    Morales, M.D.2    Reviejo, A.J.3    Hall, E.H.4    Pingarron, J.M.5
  • 170
    • 0000831938 scopus 로고
    • The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations
    • D.G. Smyth, W.H. Stein, and S. Moore The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations Journal of Biological Chemistry 238 1963 227 234
    • (1963) Journal of Biological Chemistry , vol.238 , pp. 227-234
    • Smyth, D.G.1    Stein, W.H.2    Moore, S.3
  • 174
    • 0141445947 scopus 로고    scopus 로고
    • Mammalian sulphydryl oxidase
    • J.R. Whitaker A.G.J. Voragen D.W.S. Wong Marcel Dekker New York, USA
    • H.E. Swaisgood Mammalian sulphydryl oxidase J.R. Whitaker A.G.J. Voragen D.W.S. Wong Handbook of food enzymology 2003 Marcel Dekker New York, USA 539 546
    • (2003) Handbook of Food Enzymology , pp. 539-546
    • Swaisgood, H.E.1
  • 175
    • 0037137186 scopus 로고    scopus 로고
    • Stabilization of protein by replacement of a fluctuation loop: Structural analysis of a chimera of bovine α-lactalbumin and equine lysozyme
    • M. Tada, Y. Kobashigawa, M. Mizuguchi, K. Miura, T. Kouno, and Y. Kumaki Stabilization of protein by replacement of a fluctuation loop: Structural analysis of a chimera of bovine α-lactalbumin and equine lysozyme Biochemistry 41 2002 13807 13813
    • (2002) Biochemistry , vol.41 , pp. 13807-13813
    • Tada, M.1    Kobashigawa, Y.2    Mizuguchi, M.3    Miura, K.4    Kouno, T.5    Kumaki, Y.6
  • 178
    • 33645390712 scopus 로고
    • The phosphatase test of Aschaffenburg and Mullen: Use of permanent colour standards and comparison with the Kay-Graham test
    • J. Tramer, and J. Wight The phosphatase test of Aschaffenburg and Mullen: Use of permanent colour standards and comparison with the Kay-Graham test Journal of Dairy Research 17 1950 194 199
    • (1950) Journal of Dairy Research , vol.17 , pp. 194-199
    • Tramer, J.1    Wight, J.2
  • 179
    • 0032817517 scopus 로고    scopus 로고
    • Milk alkaline phosphatase purification and production of polyclonal antibodies
    • A.V. Vega-Warner, C.-H. Wang, D.M. Smith, and Z. Ustunol Milk alkaline phosphatase purification and production of polyclonal antibodies Journal of Food Science 64 1999 601 605
    • (1999) Journal of Food Science , vol.64 , pp. 601-605
    • Vega-Warner, A.V.1    Wang, C.-H.2    Smith, D.M.3    Ustunol, Z.4
  • 180
    • 0033807437 scopus 로고    scopus 로고
    • Immune components of porcine mammary gland secretions
    • E.L. Wagstrom, K.J. Yoon, and J.J. Zimmerman Immune components of porcine mammary gland secretions Viral Immunology 13 2000 383 397
    • (2000) Viral Immunology , vol.13 , pp. 383-397
    • Wagstrom, E.L.1    Yoon, K.J.2    Zimmerman, J.J.3
  • 181
    • 5444259968 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure on conformational changes of canine milk lysozyme between the native, molten globule and unfolded states
    • M. Watanabe, T. Aizawa, M. Demura, and K. Nitta Effect of hydrostatic pressure on conformational changes of canine milk lysozyme between the native, molten globule and unfolded states Biochimica et Biophysica Acta 1702 2004 129 136
    • (2004) Biochimica et Biophysica Acta , vol.1702 , pp. 129-136
    • Watanabe, M.1    Aizawa, T.2    Demura, M.3    Nitta, K.4
  • 182
    • 0025840413 scopus 로고
    • Mutation of a single amino acid converts germ cell alkaline phosphatase to placental alkaline phosphatase
    • T. Watanabe, N. Wade, E.E. Kim, H.W. Wyekoff, and J.Y. Chou Mutation of a single amino acid converts germ cell alkaline phosphatase to placental alkaline phosphatase Journal of Biological Chemistry 266 1991 21174 21178
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 21174-21178
    • Watanabe, T.1    Wade, N.2    Kim, E.E.3    Wyekoff, H.W.4    Chou, J.Y.5
  • 186
    • 0011484826 scopus 로고
    • Reactivation of milk phosphatase following heat treatment. I
    • R.C. Wright, and J. Tramer Reactivation of milk phosphatase following heat treatment. I Journal of Dairy Research 20 1953 177 188
    • (1953) Journal of Dairy Research , vol.20 , pp. 177-188
    • Wright, R.C.1    Tramer, J.2
  • 187
    • 33645380686 scopus 로고
    • Reactivation of milk phosphatase following heat treatment. II
    • R.C. Wright, and J. Tramer Reactivation of milk phosphatase following heat treatment. II Journal of Dairy Research 20 1953 258 273
    • (1953) Journal of Dairy Research , vol.20 , pp. 258-273
    • Wright, R.C.1    Tramer, J.2
  • 188
    • 33645396079 scopus 로고
    • Reactivation of milk phosphatase following heat treatment. III
    • R.C. Wright, and J. Tramer Reactivation of milk phosphatase following heat treatment. III Journal of Dairy Research 21 1954 37 49
    • (1954) Journal of Dairy Research , vol.21 , pp. 37-49
    • Wright, R.C.1    Tramer, J.2
  • 189
    • 33645385974 scopus 로고
    • Reactivation of milk phosphatase following heat treatment. IV
    • R.C. Wright, and J. Tramer Reactivation of milk phosphatase following heat treatment. IV Journal of Dairy Research 23 1956 248 256
    • (1956) Journal of Dairy Research , vol.23 , pp. 248-256
    • Wright, R.C.1    Tramer, J.2
  • 191
    • 33645416413 scopus 로고
    • Use of butanol in the purification of the alkaline phosphatase of bovine milk
    • C.A. Zittle, and E.S. DellaMonica Use of butanol in the purification of the alkaline phosphatase of bovine milk Archives Biochemistry and Biophysics 35 1952 321 325
    • (1952) Archives Biochemistry and Biophysics , vol.35 , pp. 321-325
    • Zittle, C.A.1    Dellamonica, E.S.2
  • 192
    • 0038963630 scopus 로고
    • The fat-globule membrane of milk, alkaline phosphatase and xanthine oxidase in skim milk and cream
    • C.A. Zittle, E.S. DellaMonica, J.H. Custer, and R.K. Rudd The fat-globule membrane of milk, alkaline phosphatase and xanthine oxidase in skim milk and cream Journal of Dairy Science 39 1956 528 535
    • (1956) Journal of Dairy Science , vol.39 , pp. 528-535
    • Zittle, C.A.1    Dellamonica, E.S.2    Custer, J.H.3    Rudd, R.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.