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Volumn 101, Issue 3, 2007, Pages 1263-1271

Effect of dephosphorylation on bovine casein

Author keywords

Bovine casein; Dephosphorylation; Casein; Casein

Indexed keywords

BETA CASEIN; CASEIN;

EID: 33748986753     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2006.03.033     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 0033962437 scopus 로고    scopus 로고
    • Post-translational phosphorylation affects the IgE binding capacity of caseins
    • Bernard H., Meisel H., Creminon C., and Wal J.M. Post-translational phosphorylation affects the IgE binding capacity of caseins. FEBS Letters 467 2-3 (2000) 239-244
    • (2000) FEBS Letters , vol.467 , Issue.2-3 , pp. 239-244
    • Bernard, H.1    Meisel, H.2    Creminon, C.3    Wal, J.M.4
  • 2
    • 0017278634 scopus 로고
    • Removal of phosphate groups from casein with potato acid phosphatase
    • Bingham E.W., Farrell Jr. H.M., and Dahl K.J. Removal of phosphate groups from casein with potato acid phosphatase. Biochimica et Biophysica Acta 429 2 (1976) 448-460
    • (1976) Biochimica et Biophysica Acta , vol.429 , Issue.2 , pp. 448-460
    • Bingham, E.W.1    Farrell Jr., H.M.2    Dahl, K.J.3
  • 3
    • 0000285239 scopus 로고    scopus 로고
    • Separation and quantification of bovine milk proteins by reverse-phase high performance liquid chromatography
    • Bobe G., Beitz D.C., Freeman A.E., and Lindberg G.L. Separation and quantification of bovine milk proteins by reverse-phase high performance liquid chromatography. Journal of Agricultural and Food Chemistry 46 2 (1998) 458-463
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.2 , pp. 458-463
    • Bobe, G.1    Beitz, D.C.2    Freeman, A.E.3    Lindberg, G.L.4
  • 4
    • 0009181799 scopus 로고
    • Hydrolysis of milk proteins by immobilized Streptomyces griseus pronase
    • Church F.C., Catignani G., and Swaisgood H.E. Hydrolysis of milk proteins by immobilized Streptomyces griseus pronase. Journal of Dairy Science 64 5 (1981) 724-731
    • (1981) Journal of Dairy Science , vol.64 , Issue.5 , pp. 724-731
    • Church, F.C.1    Catignani, G.2    Swaisgood, H.E.3
  • 5
    • 84872883032 scopus 로고    scopus 로고
    • Coker, C.J. (1991). Proteolysis in cheese: A review. NZDR1 Report PC91R908. New Zealand Dairy Research, Palmerston North.
  • 6
  • 8
    • 0006263605 scopus 로고    scopus 로고
    • Milk proteins
    • Fox P.F., and McSweeney P.L.H. (Eds), Blackie Academic & Professional, London (UK)
    • Fox P.F., and McSweeney P.L.H. Milk proteins. In: Fox P.F., and McSweeney P.L.H. (Eds). Dairy chemistry and biochemistry (1998), Blackie Academic & Professional, London (UK) 146-186
    • (1998) Dairy chemistry and biochemistry , pp. 146-186
    • Fox, P.F.1    McSweeney, P.L.H.2
  • 9
    • 0015384891 scopus 로고
    • Determination of protein: A modification of the Lowry method that gives a linear photometric response
    • Hartree E.F. Determination of protein: A modification of the Lowry method that gives a linear photometric response. Analytical Biochemistry 48 2 (1972) 422-427
    • (1972) Analytical Biochemistry , vol.48 , Issue.2 , pp. 422-427
    • Hartree, E.F.1
  • 10
    • 4944232026 scopus 로고    scopus 로고
    • Detection of phosphorylated peptides in proteomic analyses using microfluidic compact disk technology
    • Hirschberg D., Jagerbrink T., Samskog J., Gustafsson M., Stahlberg M., Alvelius G., et al. Detection of phosphorylated peptides in proteomic analyses using microfluidic compact disk technology. Analytical Chemistry 76 19 (2004) 5864-5871
    • (2004) Analytical Chemistry , vol.76 , Issue.19 , pp. 5864-5871
    • Hirschberg, D.1    Jagerbrink, T.2    Samskog, J.3    Gustafsson, M.4    Stahlberg, M.5    Alvelius, G.6
  • 11
    • 0023689754 scopus 로고
    • Primary and predicted secondary structures of the caseins in relation to their biological functions
    • Holt C., and Sawyer L. Primary and predicted secondary structures of the caseins in relation to their biological functions. Protein Engineering 2 4 (1988) 241-259
    • (1988) Protein Engineering , vol.2 , Issue.4 , pp. 241-259
    • Holt, C.1    Sawyer, L.2
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 5259 (1970) 680-685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0035122684 scopus 로고    scopus 로고
    • On-membrane digestion of β-casein for determination of phosphorylation sites by matrix-assisted laser desorption/ionization quadrupole/time-of-flight mass spectrometry
    • Lee C.H., McComb M.E., Bromirski M., Jilkine A., Ens W., Standing K.G., et al. On-membrane digestion of β-casein for determination of phosphorylation sites by matrix-assisted laser desorption/ionization quadrupole/time-of-flight mass spectrometry. Rapid Communications in Mass Spectrometry 15 3 (2001) 191-202
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , Issue.3 , pp. 191-202
    • Lee, C.H.1    McComb, M.E.2    Bromirski, M.3    Jilkine, A.4    Ens, W.5    Standing, K.G.6
  • 15
    • 21844511439 scopus 로고
    • Analysis of major bovine milk proteins by on-line high-performace liquid chromatography and Electrospray ionization-mass spectrometry
    • Léonil J., Mollé D., Gaucheron F., Arpino P., Guénot P., and Maubois J.L. Analysis of major bovine milk proteins by on-line high-performace liquid chromatography and Electrospray ionization-mass spectrometry. Lait 75 (1995) 193-210
    • (1995) Lait , vol.75 , pp. 193-210
    • Léonil, J.1    Mollé, D.2    Gaucheron, F.3    Arpino, P.4    Guénot, P.5    Maubois, J.L.6
  • 16
    • 0024368356 scopus 로고
    • Enzymatic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula
    • Li-Chan E., and Nakai S. Enzymatic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula. Journal of Dairy Research 56 3 (1989) 381-390
    • (1989) Journal of Dairy Research , vol.56 , Issue.3 , pp. 381-390
    • Li-Chan, E.1    Nakai, S.2
  • 17
    • 6344277278 scopus 로고    scopus 로고
    • Purification and identification of water-soluble phosphopeptides from cheese using Fe (III) affinity chromatography and mass spectrometry
    • Lund M., and Ardö Y. Purification and identification of water-soluble phosphopeptides from cheese using Fe (III) affinity chromatography and mass spectrometry. Journal of Agricultural and Food Chemistry 52 21 (2004) 6616-6622
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.21 , pp. 6616-6622
    • Lund, M.1    Ardö, Y.2
  • 19
    • 24944571601 scopus 로고    scopus 로고
    • Milk proteins. Heterogeneity, fractionation and isolation
    • Roginski H., Faquay J.W., and Fox P.F. (Eds), Academic Press, New York
    • Ng-Kwai-Hang K.F. Milk proteins. Heterogeneity, fractionation and isolation. In: Roginski H., Faquay J.W., and Fox P.F. (Eds). Encyclopedia of dairy science vol. 3 (2003), Academic Press, New York 1881-1894
    • (2003) Encyclopedia of dairy science , vol.3 , pp. 1881-1894
    • Ng-Kwai-Hang, K.F.1
  • 21
    • 0028540586 scopus 로고
    • Determination of total phosphorus in food by colorimetric measurement of phosphorus as molybdenum blue after dry-ashing: NMKL interlaboratory study
    • Pulliainen K.T., and Wallin H.C. Determination of total phosphorus in food by colorimetric measurement of phosphorus as molybdenum blue after dry-ashing: NMKL interlaboratory study. Journal of AOAC International 77 6 (1994) 1557-1561
    • (1994) Journal of AOAC International , vol.77 , Issue.6 , pp. 1557-1561
    • Pulliainen, K.T.1    Wallin, H.C.2
  • 22
    • 0031795358 scopus 로고    scopus 로고
    • Enzyme applications for agro-processing in developing countries: An inventory of current and potential applications
    • Rolle R.S. Enzyme applications for agro-processing in developing countries: An inventory of current and potential applications. World Journal of Microbiology and Biotechnology 14 5 (1998) 611-619
    • (1998) World Journal of Microbiology and Biotechnology , vol.14 , Issue.5 , pp. 611-619
    • Rolle, R.S.1
  • 23
    • 0000529133 scopus 로고
    • Casein association and micelle formation
    • Fox P.F. (Ed), Elsevier, London
    • Rollema H.S. Casein association and micelle formation. In: Fox P.F. (Ed). Advanced dairy chemistry vol. 1 (1992), Elsevier, London 111-140
    • (1992) Advanced dairy chemistry , vol.1 , pp. 111-140
    • Rollema, H.S.1
  • 24
    • 84905387178 scopus 로고    scopus 로고
    • Milk proteins/functional properties
    • Roginski H., Faquay J.W., and Fox P.F. (Eds), Academic Press, New York
    • Singh H. Milk proteins/functional properties. In: Roginski H., Faquay J.W., and Fox P.F. (Eds). Encyclopedia of dairy science vol. 3 (2003), Academic Press, New York 1976-1982
    • (2003) Encyclopedia of dairy science , vol.3 , pp. 1976-1982
    • Singh, H.1
  • 25
  • 27
    • 84972837662 scopus 로고
    • Qualitative and quantitative determination of caseins with reverse-phase and anion exchange HPLC
    • Strange E.D., van Hekken D., and Thompson M.P. Qualitative and quantitative determination of caseins with reverse-phase and anion exchange HPLC. Journal of Food Science 56 5 (1991) 1415-1420
    • (1991) Journal of Food Science , vol.56 , Issue.5 , pp. 1415-1420
    • Strange, E.D.1    van Hekken, D.2    Thompson, M.P.3
  • 28
    • 0001662870 scopus 로고
    • Chemistry of milk proteins
    • Fox P.F. (Ed), Applied Science Publishers, New York
    • Swaisgood H.E. Chemistry of milk proteins. In: Fox P.F. (Ed). Developments in dairy chemistry vol. 1 (1982), Applied Science Publishers, New York 1-60
    • (1982) Developments in dairy chemistry , vol.1 , pp. 1-60
    • Swaisgood, H.E.1
  • 29
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • Fox P.F. (Ed), Elsevier, London
    • Swaisgood H.E. Chemistry of the caseins. In: Fox P.F. (Ed). Advanced dairy chemistry vol. 1 (1992), Elsevier, London 63-110
    • (1992) Advanced dairy chemistry , vol.1 , pp. 63-110
    • Swaisgood, H.E.1
  • 30
    • 21344496463 scopus 로고
    • Functional properties of dephosphorylated bovine whole casein
    • van Hekken D.L., and Strange E.D. Functional properties of dephosphorylated bovine whole casein. Journal of Dairy Science 76 11 (1993) 3384-3391
    • (1993) Journal of Dairy Science , vol.76 , Issue.11 , pp. 3384-3391
    • van Hekken, D.L.1    Strange, E.D.2
  • 31
    • 0037162919 scopus 로고    scopus 로고
    • Separation and quantification of the major casein fractions by reverse-phase high-performance liquid chromatography and urea-polyacrylamide gel electrophoresis detection of milk adulterations
    • Veloso A.C.A., Teixeira N., and Ferreira I.M.P.C. Separation and quantification of the major casein fractions by reverse-phase high-performance liquid chromatography and urea-polyacrylamide gel electrophoresis detection of milk adulterations. Journal of Chromatography A 967 2 (2002) 209-218
    • (2002) Journal of Chromatography A , vol.967 , Issue.2 , pp. 209-218
    • Veloso, A.C.A.1    Teixeira, N.2    Ferreira, I.M.P.C.3
  • 34
    • 0017183409 scopus 로고
    • A study of the enzymatic dephosphorylation of β-casein and derived phosphopeptide
    • West D.W., and Towers G.E. A study of the enzymatic dephosphorylation of β-casein and derived phosphopeptide. Biochimica et Biophysica Acta 435 2 (1976) 383-390
    • (1976) Biochimica et Biophysica Acta , vol.435 , Issue.2 , pp. 383-390
    • West, D.W.1    Towers, G.E.2
  • 35
    • 0022715280 scopus 로고
    • Structure and function of the phosphorylated residues of casein
    • West D.W. Structure and function of the phosphorylated residues of casein. Journal of Dairy Research 53 (1986) 333-352
    • (1986) Journal of Dairy Research , vol.53 , pp. 333-352
    • West, D.W.1
  • 37
    • 5044222901 scopus 로고    scopus 로고
    • Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis
    • Zhong H., Zhang Y., Wen Z., and Li L. Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis. Nature Biotechnology 22 10 (2004) 1291-1296
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1291-1296
    • Zhong, H.1    Zhang, Y.2    Wen, Z.3    Li, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.