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Volumn 343, Issue 2, 2006, Pages 450-458

Disulphide bonds in casein micelle from milk

Author keywords

Caseins; Disulphide bond; Epithelial cells; Mammary gland; Milk proteins

Indexed keywords

CASEIN;

EID: 33645117655     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.03.005     Document Type: Article
Times cited : (25)

References (25)
  • 1
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • P.F. Fox P.L.H. McSweeney Kluwer academic/Plenum publishers Dordrecht/New York
    • C.G. De Kruif, and C. Holt Casein micelle structure, functions and interactions P.F. Fox P.L.H. McSweeney Advanced dairy chemistry 2003 Kluwer academic/Plenum publishers Dordrecht/New York 233 276
    • (2003) Advanced Dairy Chemistry , pp. 233-276
    • De Kruif, C.G.1    Holt, C.2
  • 2
    • 0027408422 scopus 로고
    • Transport of casein submicelles and formation of secretion granules in the Golgi apparatus of epithelial cells of the lactating mammary gland of the rat
    • Y. Clermont, L. Xia, A. Rambourg, J.D. Turner, and L. Hermo Transport of casein submicelles and formation of secretion granules in the Golgi apparatus of epithelial cells of the lactating mammary gland of the rat Anat. Rec. 235 1993 363 373
    • (1993) Anat. Rec. , vol.235 , pp. 363-373
    • Clermont, Y.1    Xia, L.2    Rambourg, A.3    Turner, J.D.4    Hermo, L.5
  • 3
    • 0032703108 scopus 로고    scopus 로고
    • Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells
    • E. Chanat, P. Martin, and M. Ollivier-Bousquet Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells J. Cell Sci. 112 Pt. 19 1999 3399 3412
    • (1999) J. Cell Sci. , vol.112 , Issue.19 PART , pp. 3399-3412
    • Chanat, E.1    Martin, P.2    Ollivier-Bousquet, M.3
  • 4
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure in dairy products
    • D.S. Horne Casein interactions: casting light on the black boxes, the structure in dairy products Int. Dairy J. 8 1998 171 177
    • (1998) Int. Dairy J. , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 6
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 8
    • 0028916539 scopus 로고
    • Synthesis and secretion of caseins by the mouse mammary gland: Production and characterization of new polyclonal antibodies
    • I. Barash, A. Faerman, R. Puzis, D. Peterson, and M. Shani Synthesis and secretion of caseins by the mouse mammary gland: production and characterization of new polyclonal antibodies Mol. Cell. Biochem. 144 1995 175 180
    • (1995) Mol. Cell. Biochem. , vol.144 , pp. 175-180
    • Barash, I.1    Faerman, A.2    Puzis, R.3    Peterson, D.4    Shani, M.5
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels
    • J. Heukeshoven, and R. Dernick Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels Electrophoresis 9 1988 28 32
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 11
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 12
    • 0026552375 scopus 로고
    • Reexamination of the polymeric distributions of kappa-casein isolated from bovine milk
    • M.L. Groves, H.J. Dower, and H.M. Farrell Jr. Reexamination of the polymeric distributions of kappa-casein isolated from bovine milk J. Protein Chem. 11 1992 21 28
    • (1992) J. Protein Chem. , vol.11 , pp. 21-28
    • Groves, M.L.1    Dower, H.J.2    Farrell Jr., H.M.3
  • 13
    • 0026683462 scopus 로고
    • The multimeric structure and disulfide-bonding pattern of bovine kappa-casein
    • L.K. Rasmussen, P. Hojrup, and T.E. Petersen The multimeric structure and disulfide-bonding pattern of bovine kappa-casein Eur. J. Biochem. 207 1992 215 222
    • (1992) Eur. J. Biochem. , vol.207 , pp. 215-222
    • Rasmussen, L.K.1    Hojrup, P.2    Petersen, T.E.3
  • 16
    • 0000611538 scopus 로고
    • Etude des relations entre les caractéristiques physico-chimiques des laits de chèvre et leur aptitude à la coagulation par la présure
    • F. Remeuf, J. Lenoir, and C. Duby Etude des relations entre les caractéristiques physico-chimiques des laits de chèvre et leur aptitude à la coagulation par la présure Lait 69 1989
    • (1989) Lait , vol.69
    • Remeuf, F.1    Lenoir, J.2    Duby, C.3
  • 17
    • 0026605009 scopus 로고
    • Localization of two interchain disulfide bridges in dimers of bovine alpha s2-casein. Parallel and antiparallel alignments of the polypeptide chains
    • L.K. Rasmussen, P. Hojrup, and T.E. Petersen Localization of two interchain disulfide bridges in dimers of bovine alpha s2-casein. Parallel and antiparallel alignments of the polypeptide chains Eur. J. Biochem. 203 1992 381 386
    • (1992) Eur. J. Biochem. , vol.203 , pp. 381-386
    • Rasmussen, L.K.1    Hojrup, P.2    Petersen, T.E.3
  • 19
    • 0026668858 scopus 로고
    • Structure and stability of bovine casein micelles
    • J.T. Edall C.B. Anfimsen F.M. Richards D.S. Eisenberg Academic Press San Diego
    • C. Holt Structure and stability of bovine casein micelles J.T. Edall C.B. Anfimsen F.M. Richards D.S. Eisenberg Adv. Protein Chem. 1992 Academic Press San Diego 63 151
    • (1992) Adv. Protein Chem. , pp. 63-151
    • Holt, C.1
  • 20
    • 0028557973 scopus 로고
    • Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine kappa-casein
    • A. Pisano, N.H. Packer, J.W. Redmond, K.L. Williams, and A.A. Gooley Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine kappa-casein Glycobiology 4 1994 837 844
    • (1994) Glycobiology , vol.4 , pp. 837-844
    • Pisano, A.1    Packer, N.H.2    Redmond, J.W.3    Williams, K.L.4    Gooley, A.A.5
  • 22
    • 0021248179 scopus 로고
    • SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins
    • E. Kaufmann, N. Geisler, and K. Weber SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins FEBS Lett. 170 1984 81 84
    • (1984) FEBS Lett. , vol.170 , pp. 81-84
    • Kaufmann, E.1    Geisler, N.2    Weber, K.3
  • 23
    • 0023332890 scopus 로고
    • The primary structure of human secretogranin I (chromogranin B): Comparison with chromogranin a reveals homologous terminal domains and a large intervening variable region
    • U.M. Benedum, A. Lamouroux, D.S. Konecki, P. Rosa, A. Hille, P.A. Baeuerle, R. Frank, F. Lottspeich, J. Mallet, and W.B. Huttner The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region EMBO J. 6 1987 1203 1211
    • (1987) EMBO J. , vol.6 , pp. 1203-1211
    • Benedum, U.M.1    Lamouroux, A.2    Konecki, D.S.3    Rosa, P.4    Hille, A.5    Baeuerle, P.A.6    Frank, R.7    Lottspeich, F.8    Mallet, J.9    Huttner, W.B.10
  • 24
    • 0028672753 scopus 로고
    • The granin protein family: Markers for neuroendocrine cells and tools for the diagnosis of neuroendocrine tumors
    • P. Rosa, and H.-H. Gerdes The granin protein family: markers for neuroendocrine cells and tools for the diagnosis of neuroendocrine tumors J. Endocrinol. Invest. 17 1994 207 225
    • (1994) J. Endocrinol. Invest. , vol.17 , pp. 207-225
    • Rosa, P.1    Gerdes, H.-H.2
  • 25
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins: Interpretation of the primary and secondary structures of the αs1, β- And k-caseins
    • C. Holt, and L. Sawyer Caseins as rheomorphic proteins: interpretation of the primary and secondary structures of the αS1, β- and k-caseins J. Chem. Soc. Faraday Trans. 89 1993 2683 2692
    • (1993) J. Chem. Soc. Faraday Trans. , vol.89 , pp. 2683-2692
    • Holt, C.1    Sawyer, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.