메뉴 건너뛰기




Volumn 606, Issue , 2008, Pages 143-161

Milk lipoprotein membranes and their imperative enzymes

Author keywords

[No Author keywords available]

Indexed keywords

5' NUCLEOTIDASE; ALKALINE PHOSPHATASE; CYSTEINE; GLUTATHIONE; LIPOPOLYSACCHARIDE; LIPOPROTEIN; MILK FAT; MILK PROTEIN; RIBONUCLEASE;

EID: 84934440662     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-74087-4_5     Document Type: Review
Times cited : (11)

References (61)
  • 1
    • 33846994031 scopus 로고    scopus 로고
    • Antioxidant mechanism of milk mineral-High-affinity iron binding
    • Allen, K., & Cornforth, D. (2007). Antioxidant mechanism of milk mineral-High-affinity iron binding. Journal of Food Science, 72, C78-C83.
    • (2007) Journal of Food Science , vol.72
    • Allen, K.1    Cornforth, D.2
  • 2
    • 33847057326 scopus 로고    scopus 로고
    • Assessment of lactate dehydrogenase, alkaline phosphatase and aspartate aminotransferase activities in cow's milk as an indicator of subclinical mastitis
    • Babaei, H., Mansouri-Najand, L., Molaei, M. M., Kheradmand, A., & Sharifan, M. (2007). Assessment of lactate dehydrogenase, alkaline phosphatase and aspartate aminotransferase activities in cow's milk as an indicator of subclinical mastitis. Veterinary Research Communications, 31, 419-425.
    • (2007) Veterinary Research Communications , vol.31 , pp. 419-425
    • Babaei, H.1    Mansouri-Najand, L.2    Molaei, M.M.3    Kheradmand, A.4    Sharifan, M.5
  • 3
    • 0142179149 scopus 로고    scopus 로고
    • Calf intestinal alkaline phosphatase, a novel therapeutic drug for lipopolysaccharide (LPS)-mediated diseases, attenuates LPS toxicity in mice and piglets
    • Beumer, C., Wulferink, M., Raaben, W., Fiechter, D., Brands, R., & Seinen, W. (2003). Calf intestinal alkaline phosphatase, a novel therapeutic drug for lipopolysaccharide (LPS)-mediated diseases, attenuates LPS toxicity in mice and piglets. Journal of Pharmacology and Experimental Therapy, 307, 737-744.
    • (2003) Journal of Pharmacology and Experimental Therapy , vol.307 , pp. 737-744
    • Beumer, C.1    Wulferink, M.2    Raaben, W.3    Fiechter, D.4    Brands, R.5    Seinen, W.6
  • 4
    • 0026710226 scopus 로고
    • Alkaline phosphatase in the lactating bovine mammary gland and the milk fat globule membrane. Release by phosphatidylinositolspecific phospholipase-C
    • Bingham, E. W., & Malin, E. L. (1992). Alkaline phosphatase in the lactating bovine mammary gland and the milk fat globule membrane. Release by phosphatidylinositolspecific phospholipase-C. Comparative Biochemistry and Physiology B-Biochemistry & Molcular Biology, 102, 213-218.
    • (1992) Comparative Biochemistry and Physiology B-Biochemistry & Molcular Biology , vol.102 , pp. 213-218
    • Bingham, E.W.1    Malin, E.L.2
  • 5
    • 33748749058 scopus 로고    scopus 로고
    • High level experssion of tissue-nonspecific alkaline phosphatase in the milk of transgenic rabbits
    • Bodrogi, L., Brands, R., Roaben, W., Seinen, W., Baranyi, M., Fiechter, D., & Bosze, Z. (2006). High level experssion of tissue-nonspecific alkaline phosphatase in the milk of transgenic rabbits. Transgenic Research, 15, 627-636.
    • (2006) Transgenic Research , vol.15 , pp. 627-636
    • Bodrogi, L.1    Brands, R.2    Roaben, W.3    Seinen, W.4    Baranyi, M.5    Fiechter, D.6    Bosze, Z.7
  • 6
  • 7
    • 0026510436 scopus 로고
    • Control of neutrophils alkaline phosphatase synthesis by cytokines in health and disease
    • Chikkappa, G. (1992). Control of neutrophils alkaline phosphatase synthesis by cytokines in health and disease. Experimental Haematology, 20, 388-390.
    • (1992) Experimental Haematology , vol.20 , pp. 388-390
    • Chikkappa, G.1
  • 9
    • 13244271908 scopus 로고    scopus 로고
    • The regulation and role of extracellular glutathione peroxidase
    • Comhair, S. A. A., & Erzurum, S. C. (2005). The regulation and role of extracellular glutathione peroxidase. Antioxidant & Redox Signaling, 7, 72-79.
    • (2005) Antioxidant & Redox Signaling , vol.7 , pp. 72-79
    • Comhair, S.A.A.1    Erzurum, S.C.2
  • 10
    • 33845351359 scopus 로고    scopus 로고
    • The RNase a superfamily: Generation of diversity and innate host defense
    • Dyer, K. D., & Rosenberg, H. F. (2006). The RNase a superfamily: Generation of diversity and innate host defense. Molecular Diversity, 10, 585-597.
    • (2006) Molecular Diversity , vol.10 , pp. 585-597
    • Dyer, K.D.1    Rosenberg, H.F.2
  • 12
    • 0025312998 scopus 로고
    • Alkaline phosphatase isozymes: Recent progress
    • Fishman, H. (1990). Alkaline phosphatase isozymes: Recent progress. Clinical Biochemistry, 23, 99-104.
    • (1990) Clinical Biochemistry , vol.23 , pp. 99-104
    • Fishman, H.1
  • 13
    • 85069124377 scopus 로고    scopus 로고
    • Fox, P. F. (2003). Indigenous enzymes in milk. In P. F. Fox & P. L. H. McSweeney (Eds.), Advanced Dairy Chemistry, 1, Proteins (pp. 447-467). New York: Kluwer Academic/Plenum Publishers.
    • Fox, P. F. (2003). Indigenous enzymes in milk. In P. F. Fox & P. L. H. McSweeney (Eds.), Advanced Dairy Chemistry, Vol. 1, Proteins (pp. 447-467). New York: Kluwer Academic/Plenum Publishers.
  • 14
    • 33645407624 scopus 로고    scopus 로고
    • Indigenous enzymes in milk: Overview and historical aspects-Part 1
    • Fox, P. F., & Kelly, A. L. (2006a). Indigenous enzymes in milk: Overview and historical aspects-Part 1. International Dairy Journal, 16, 500-516.
    • (2006) International Dairy Journal , vol.16 , pp. 500-516
    • Fox, P.F.1    Kelly, A.L.2
  • 15
    • 33645393430 scopus 로고    scopus 로고
    • Indigenous enzymes in milk: Overview and historical aspects-Part 2
    • Fox, P. F., & Kelly, A. L. (2006b). Indigenous enzymes in milk: Overview and historical aspects-Part 2. International Dairy Journal, 16, 517-532.
    • (2006) International Dairy Journal , vol.16 , pp. 517-532
    • Fox, P.F.1    Kelly, A.L.2
  • 16
    • 0033816854 scopus 로고    scopus 로고
    • Ecto-enzymes: Physiology meets pathology
    • Goding, J. W. (2000). Ecto-enzymes: Physiology meets pathology. Journal of Leukocyte Biology, 67, 285-311.
    • (2000) Journal of Leukocyte Biology , vol.67 , pp. 285-311
    • Goding, J.W.1
  • 17
    • 0032409354 scopus 로고    scopus 로고
    • Molecular biology of plasma membrane redox enzymes: A survey of current knowledge
    • Goldenberg, H. (1998). Molecular biology of plasma membrane redox enzymes: A survey of current knowledge. Protoplasma, 205, 3-9.
    • (1998) Protoplasma , vol.205 , pp. 3-9
    • Goldenberg, H.1
  • 18
    • 33645391515 scopus 로고    scopus 로고
    • Milk xanthine oxidase: Properties and physiological roles
    • Harrison, R. (2006). Milk xanthine oxidase: Properties and physiological roles. International Dairy Journal, 16, 546-554.
    • (2006) International Dairy Journal , vol.16 , pp. 546-554
    • Harrison, R.1
  • 19
    • 0035993075 scopus 로고    scopus 로고
    • Glutatthione secretion into rat milk and its subsequent γ-glutamyltranspeptidase mediated catabolisim
    • Fujikake, N., & Ballatori, N. (2002). Glutatthione secretion into rat milk and its subsequent γ-glutamyltranspeptidase mediated catabolisim. Biology of the Neonate, 82, 134-138.
    • (2002) Biology of the Neonate , vol.82 , pp. 134-138
    • Fujikake, N.1    Ballatori, N.2
  • 20
    • 14844345210 scopus 로고    scopus 로고
    • Intracellular origin and secretion of milk fat globules
    • Heid, H. W., & Keenan, T. W. (2005). Intracellular origin and secretion of milk fat globules. European Journal of Cell Biology, 84, 245-258.
    • (2005) European Journal of Cell Biology , vol.84 , pp. 245-258
    • Heid, H.W.1    Keenan, T.W.2
  • 21
    • 51249192173 scopus 로고
    • Acomparative study of lipids of globule membrane and fat core and of milk serum of cows
    • Huang, T. C.,&Kuksis, A. (1967).Acomparative study of lipids of globule membrane and fat core and of milk serum of cows. Lipids, 2, 453-460.
    • (1967) Lipids , vol.2 , pp. 453-460
    • Huang, T.C.1    Kuksis, A.2
  • 22
    • 0040743999 scopus 로고
    • Secretory membranes of the lactating mammary gland
    • Kanno, C. (1990). Secretory membranes of the lactating mammary gland. Protoplasma, 159,184-208.
    • (1990) Protoplasma , vol.159 , pp. 184-208
    • Kanno, C.1
  • 23
    • 27744536412 scopus 로고    scopus 로고
    • Pho5p and newly identified nucleotide pyrophosphatases/phosphodiesterases regulate extracellular nucleotide phosphate metabolism in Saccharomyces cerevisiae
    • Kennedy, E. J., Pillus, L., & Ghosh, G. (2005). Pho5p and newly identified nucleotide pyrophosphatases/phosphodiesterases regulate extracellular nucleotide phosphate metabolism in Saccharomyces cerevisiae. Eukaryotic Cell, 4, 1892-1901.
    • (2005) Eukaryotic Cell , vol.4 , pp. 1892-1901
    • Kennedy, E.J.1    Pillus, L.2    Ghosh, G.3
  • 24
    • 0016192882 scopus 로고
    • Comparison of properties of membranes isolated from bovine skim milk and cream
    • Kitchen, B. J. (1974). Comparison of properties of membranes isolated from bovine skim milk and cream. Biochimica et Biophysica Acta, 356, 257-269.
    • (1974) Biochimica et Biophysica Acta , vol.356 , pp. 257-269
    • Kitchen, B.J.1
  • 25
  • 26
    • 1842611600 scopus 로고    scopus 로고
    • Differential effect of calcium phosphate and calcium pyrophosphate on binding of matrix metalloproteinases to fibrin: Comparison to a fibrin-binding protease from inflammatory joint fluids
    • Makowski, G. S., & Ramsby, M. L. (2004). Differential effect of calcium phosphate and calcium pyrophosphate on binding of matrix metalloproteinases to fibrin: Comparison to a fibrin-binding protease from inflammatory joint fluids. Clinical and Experimental Immunology, 136,176-187.
    • (2004) Clinical and Experimental Immunology , vol.136 , pp. 176-187
    • Makowski, G.S.1    Ramsby, M.L.2
  • 29
    • 0021098087 scopus 로고
    • Composition and ultrastructure of calcium-phosphate citrate complexes in bovine-milk systems
    • McGann, T. C., Buchheim, W., Kearney, R. D., & Richardson, T. (1983a). Composition and ultrastructure of calcium-phosphate citrate complexes in bovine-milk systems. Biochimica et Biophysica Acta, 760, 415-420.
    • (1983) Biochimica et Biophysica Acta , vol.760 , pp. 415-420
    • McGann, T.C.1    Buchheim, W.2    Kearney, R.D.3    Richardson, T.4
  • 31
    • 0034535614 scopus 로고    scopus 로고
    • Defective localization of the Wilson disease protein (ATP7B) in the mammary gland of the toxic milk mouse and the effects of copper supplementation
    • Michalczyk, A. A., Rieger, J., Allen, K. J., Mercer, J. F. B., & Ackland, M. L. (2000). Defective localization of the Wilson disease protein (ATP7B) in the mammary gland of the toxic milk mouse and the effects of copper supplementation. Biochemical Journal, 352, 565-571.
    • (2000) Biochemical Journal , vol.352 , pp. 565-571
    • Michalczyk, A.A.1    Rieger, J.2    Allen, K.J.3    Mercer, J.F.B.4    Ackland, M.L.5
  • 32
    • 0040743986 scopus 로고
    • The lipoprotein particles in cow's milk
    • Morton, R. K. (1954). The lipoprotein particles in cow's milk. Biochemical Journal, 57, 231-237.
    • (1954) Biochemical Journal , vol.57 , pp. 231-237
    • Morton, R.K.1
  • 33
    • 0242575194 scopus 로고    scopus 로고
    • The bovine neutrophil: Structure and function in blood and milk
    • Paape, M. J., Bannerman, D. D., Zhao, X., & Lee J. W. (2003). The bovine neutrophil: Structure and function in blood and milk. Veterinary Research, 34, 597-627.
    • (2003) Veterinary Research , vol.34 , pp. 597-627
    • Paape, M.J.1    Bannerman, D.D.2    Zhao, X.3    Lee, J.W.4
  • 34
    • 0014986754 scopus 로고
    • Relationship of milk phospholipids to membranes of secretory cell
    • Patton, S., & Keenan, T. W. (1971). Relationship of milk phospholipids to membranes of secretory cell. Lipids, 6, 58-68.
    • (1971) Lipids , vol.6 , pp. 58-68
    • Patton, S.1    Keenan, T.W.2
  • 35
    • 0015911754 scopus 로고
    • Plasma-membrane fragments in bovine and caprine skim milks
    • Plantz, P. E., & Patton, S. (1973). Plasma-membrane fragments in bovine and caprine skim milks. Biochimica et Biophysica Acta, 291,51-60.
    • (1973) Biochimica et Biophysica Acta , vol.291 , pp. 51-60
    • Plantz, P.E.1    Patton, S.2
  • 36
    • 0015653188 scopus 로고
    • Further evidence of plasma-membrane material in skim milk
    • Plantz, P. E., Keenan, T. W., & Patton, S. (1973). Further evidence of plasma-membrane material in skim milk. Journal of Dairy Science, 56,978-983.
    • (1973) Journal of Dairy Science , vol.56 , pp. 978-983
    • Plantz, P.E.1    Keenan, T.W.2    Patton, S.3
  • 41
    • 0006396286 scopus 로고
    • Changes in ribonuclease concentration during lactation in cow's colostrum and milk
    • Roman, M., Sanchez, L., & Calvo, M. (1990). Changes in ribonuclease concentration during lactation in cow's colostrum and milk. Netherlands Milk and Dairy Journal, 44, 207-212.
    • (1990) Netherlands Milk and Dairy Journal , vol.44 , pp. 207-212
    • Roman, M.1    Sanchez, L.2    Calvo, M.3
  • 42
    • 33846241170 scopus 로고    scopus 로고
    • Ribonucleotides: Conditionally essential nutrients shown to enhance immune function and reduce diarrheal disease in infants
    • Schallera, J. P., Bucka, R. H., & Ruedab, R. (2007). Ribonucleotides: Conditionally essential nutrients shown to enhance immune function and reduce diarrheal disease in infants. Seminars in Fetal and Neonatal Medicine, 12, 35-44.
    • (2007) Seminars in Fetal and Neonatal Medicine , vol.12 , pp. 35-44
    • Schallera, J.P.1    Bucka, R.H.2    Ruedab, R.3
  • 45
    • 0026887218 scopus 로고
    • Is the milk-fat-globule membrane a model for mammary secretory-cell apical membrane?
    • Shennan, D. B. (1992). Is the milk-fat-globule membrane a model for mammary secretory-cell apical membrane? Experimental Physiology, 77,653-656.
    • (1992) Experimental Physiology , vol.77 , pp. 653-656
    • Shennan, D.B.1
  • 46
    • 0021230083 scopus 로고
    • Co-localization of superoxide generation and NADP formation in plasma-membrane fractions from human-neutrophils
    • Shirley, P. S., Bass, D. A., Lees, C. J., Parce, J. W., Waite, B. M., & Dechatelet, L. R. (1984). Co-localization of superoxide generation and NADP formation in plasma-membrane fractions from human-neutrophils. Inflammation, 8, 323-335.
    • (1984) Inflammation , vol.8 , pp. 323-335
    • Shirley, P.S.1    Bass, D.A.2    Lees, C.J.3    Parce, J.W.4    Waite, B.M.5    Dechatelet, L.R.6
  • 47
    • 0035858127 scopus 로고    scopus 로고
    • Neonatal and early life vaccinology
    • Siegrist, C. A. (2001). Neonatal and early life vaccinology. Vaccine, 19, 3331-3346.
    • (2001) Vaccine , vol.19 , pp. 3331-3346
    • Siegrist, C.A.1
  • 48
    • 34447647821 scopus 로고    scopus 로고
    • Distribution of xanthine oxidase and xanthine dehydrogenase activity in bovine milk: Physiological and technological implications
    • Silanikove, N., & Shapiro, F. (2007). Distribution of xanthine oxidase and xanthine dehydrogenase activity in bovine milk: Physiological and technological implications. International Dairy Journal, 17,1188-1194.
    • (2007) International Dairy Journal , vol.17 , pp. 1188-1194
    • Silanikove, N.1    Shapiro, F.2
  • 49
    • 0034703510 scopus 로고    scopus 로고
    • Stress down regulates milk yield in cows by plasmin induced beta-casein product that blocks Kp channels on the apical membranes
    • Silanikove, N., Shamay, A., Shinder, D., & Moran, A. (2000). Stress down regulates milk yield in cows by plasmin induced beta-casein product that blocks Kp channels on the apical membranes. Life Sciences, 67, 2201-2212.
    • (2000) Life Sciences , vol.67 , pp. 2201-2212
    • Silanikove, N.1    Shamay, A.2    Shinder, D.3    Moran, A.4
  • 50
    • 15944398704 scopus 로고    scopus 로고
    • Role of xanthine oxidase, lactoperoxidase, andNOin the innate immune system of mammary secretion during active involution in dairy cows: Manipulation with casein hydrolysates
    • Silanikove, N., Shapiro, F., Shamay, A., & Leitner, G. (2005). Role of xanthine oxidase, lactoperoxidase, andNOin the innate immune system of mammary secretion during active involution in dairy cows: Manipulation with casein hydrolysates. Free Radical Biology Medicine, 38, 1139-1151.
    • (2005) Free Radical Biology Medicine , vol.38 , pp. 1139-1151
    • Silanikove, N.1    Shapiro, F.2    Shamay, A.3    Leitner, G.4
  • 51
    • 33645406062 scopus 로고    scopus 로고
    • Physiological role of indigenous milk enzymes: An overview of an evolving picture
    • Silanikove, N., Merin, U., & Leitner, G. (2006). Physiological role of indigenous milk enzymes: An overview of an evolving picture. International Dairy Journal, 16, 533-545.
    • (2006) International Dairy Journal , vol.16 , pp. 533-545
    • Silanikove, N.1    Merin, U.2    Leitner, G.3
  • 53
    • 2442637545 scopus 로고    scopus 로고
    • Perspective on the structure and function of caseins and casein micelles
    • Smith, E., Glegg, R. A.,&Holt, C. (2004). Perspective on the structure and function of caseins and casein micelles. International Journal of Dairy Technology, 157, 121-126.
    • (2004) International Journal of Dairy Technology , vol.157 , pp. 121-126
    • Smith, E.1    Glegg, R.A.2    Holt, C.3
  • 55
    • 0034813884 scopus 로고    scopus 로고
    • Inorganic pyrophosphate generation and disposition in pathophysiology
    • Terkeltaub, R. A. (2001). Inorganic pyrophosphate generation and disposition in pathophysiology. American Journal of Physiology-Cell Physiology, 281, C1- C11.
    • (2001) American Journal of Physiology-Cell Physiology , vol.281
    • Terkeltaub, R.A.1
  • 58
    • 0037082120 scopus 로고    scopus 로고
    • In vivo reversal of glutathione deficiency and susceptibility to in vivo dexamethasone-induced apoptosis by N-acetylcysteine and L-2-oxothiazolidine4-carboxylic acid, but not ascorbic acid, in thymocytes from γ-glutamyltranspeptidase-deficient knockout
    • Will, Y., Kaetzel, R. S., Brown, M. K., Fraley, T. S., & Reed, D. J. (2002). In vivo reversal of glutathione deficiency and susceptibility to in vivo dexamethasone-induced apoptosis by N-acetylcysteine and L-2-oxothiazolidine4-carboxylic acid, but not ascorbic acid, in thymocytes from γ-glutamyltranspeptidase-deficient knockout. Archives of Biochemistry and Biophysics, 397,399-406.
    • (2002) Archives of Biochemistry and Biophysics , vol.397 , pp. 399-406
    • Will, Y.1    Kaetzel, R.S.2    Brown, M.K.3    Fraley, T.S.4    Reed, D.J.5
  • 59
    • 0001792446 scopus 로고
    • Comparative mammary fine structure
    • M. Peaker Ed, New York: Academic Press
    • Wooding, F. B. P. (1977). Comparative mammary fine structure. In M. Peaker (Ed.), Comparative Aspects of Lactation (pp. 1-41). New York: Academic Press.
    • (1977) Comparative Aspects of Lactation , pp. 1-41
    • Wooding, F.B.P.1
  • 60
    • 0036109203 scopus 로고    scopus 로고
    • A novel role of alkaline phosphatase in protection from immunological liver injury in mice
    • Xu, Q., Lu, Z., & Zhang, X. (2002). A novel role of alkaline phosphatase in protection from immunological liver injury in mice. Liver, 22, 8-14.
    • (2002) Liver , vol.22 , pp. 8-14
    • Xu, Q.1    Lu, Z.2    Zhang, X.3
  • 61
    • 0034622997 scopus 로고    scopus 로고
    • First demonstration of lactoribonuclease, a ribonuclease from bovine milk with similarity to bovine pancreatic ribonuclease
    • Ye, X. Y., & Ng, T. B. (2000). First demonstration of lactoribonuclease, a ribonuclease from bovine milk with similarity to bovine pancreatic ribonuclease. Life Sciences, 67, 2025-2032.
    • (2000) Life Sciences , vol.67 , pp. 2025-2032
    • Ye, X.Y.1    Ng, T.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.