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Volumn 81, Issue 11, 1998, Pages 3004-3012

Micelle Stability: κ-Casein Structure and Function

Author keywords

Casein micelle; Glycomacropeptide structure; casein structure

Indexed keywords

CASEIN; CHYMOSIN;

EID: 0032197009     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(98)75864-3     Document Type: Article
Times cited : (82)

References (38)
  • 3
    • 0011438559 scopus 로고
    • Some aspects of casein micelle structure
    • Interactions in Food Proteins. N. Parris and R. Barford, ed. Am. Chem. Soc., Washington, DC
    • Creamer, L. K. 1991. Some aspects of casein micelle structure. Pages 148-163 in Interactions in Food Proteins. N. Parris and R. Barford, ed. ACS Symp. Ser. 454. Am. Chem. Soc., Washington, DC.
    • (1991) ACS Symp. Ser. , vol.454 , pp. 148-163
    • Creamer, L.K.1
  • 6
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H. J., and P. E. Wright. 1991. Defining solution conformations of small linear peptides. Ann. Rev. Biophys. Biophys. Chem. 20:519-538.
    • (1991) Ann. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 7
  • 8
    • 0242674074 scopus 로고    scopus 로고
    • Bovine κ-casein G: Detection, occurrence, molecular genetic characterisation, genotyping and coagulation properties
    • Int. Dairy Fed. Int. Dairy Fed., Brussels, Belgium
    • Erhardt, G., E.-M. Prinzenberg, J. Buchberger, H. Krick-Saleck, I. Krause, and M. Müller. 1998 Bovine κ-casein G: detection, occurrence, molecular genetic characterisation, genotyping and coagulation properties. Pages 328-329 in Milk Protein Polymorphism. Int. Dairy Fed. Special Issue 9702. Int. Dairy Fed., Brussels, Belgium.
    • (1998) Milk Protein Polymorphism , Issue.9702 SPEC. ISSUE , pp. 328-329
    • Erhardt, G.1    Prinzenberg, E.-M.2    Buchberger, J.3    Krick-Saleck, H.4    Krause, I.5    Müller, M.6
  • 9
    • 0026497631 scopus 로고
    • Chymosin: A short review on foetal and neonatal gastric proteases
    • Foltmann, B. 1992. Chymosin: a short review on foetal and neonatal gastric proteases. Scand. J. Clin. Lab. Invest. 52: 65-79.
    • (1992) Scand. J. Clin. Lab. Invest. , vol.52 , pp. 65-79
    • Foltmann, B.1
  • 10
    • 0022629004 scopus 로고
    • Identification of human milk kappa-casein on polyacrylamide gels by differential staining with Ethyl-Stains-all and chymosin sensitivity
    • Green, M. R. 1986. Identification of human milk kappa-casein on polyacrylamide gels by differential staining with Ethyl-Stains-all and chymosin sensitivity. J. Histochem. Cytochem. 34:147-150.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 147-150
    • Green, M.R.1
  • 11
    • 0000574723 scopus 로고
    • Effect of alcohols on the structure of caseins: Circular dichroism studies of κ-casein A
    • Griffin, M.C.A., J. C. Price, and S. R. Martin. 1986. Effect of alcohols on the structure of caseins: circular dichroism studies of κ-casein A. Int. J. Biol. Macromol. 8:367-371.
    • (1986) Int. J. Biol. Macromol. , vol.8 , pp. 367-371
    • Griffin, M.C.A.1    Price, J.C.2    Martin, S.R.3
  • 13
    • 0029588554 scopus 로고
    • High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Y. Kuroda, T. Tanaka, and Y. Goto. 1995. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol. 254:737-746.
    • (1995) J. Mol. Biol. , vol.254 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Tanaka, T.3    Goto, Y.4
  • 14
    • 0026668858 scopus 로고
    • Structure and stability of casein micelles
    • Holt, C. 1992. Structure and stability of casein micelles. Adv. Prot. Chem. 43:63-151.
    • (1992) Adv. Prot. Chem. , vol.43 , pp. 63-151
    • Holt, C.1
  • 15
    • 0023689754 scopus 로고
    • Primary and predicted secondary structures of the caseins in relation to their biological functions
    • Holt, C., and L. Sawyer. 1988. Primary and predicted secondary structures of the caseins in relation to their biological functions. Prot. Eng. 2:251-259.
    • (1988) Prot. Eng. , vol.2 , pp. 251-259
    • Holt, C.1    Sawyer, L.2
  • 18
    • 0030941296 scopus 로고    scopus 로고
    • NMR structure of a de novo designed, peptide 33mer with two distinct, compact β-sheet folds
    • Ilyina, E., V. Roongta, and K. H. Mayo. 1997. NMR structure of a de novo designed, peptide 33mer with two distinct, compact β-sheet folds. Biochemistry 36:5245-5250.
    • (1997) Biochemistry , vol.36 , pp. 5245-5250
    • Ilyina, E.1    Roongta, V.2    Mayo, K.H.3
  • 19
    • 0345160193 scopus 로고
    • Hydrolysis of κ-casein variants A, B and C by chymosin
    • Melbourne, 18-22 September 1994. Aust. Natl. Comm. Int. Dairy Fed., Glen Iris, Victoria, Australia
    • Jakob, E., C. Sievert, and Z. Puhan. 1994. Hydrolysis of κ-casein variants A, B and C by chymosin. Page 207 in Brief Commun. XXIV Int. Dairy Congr., Melbourne, 18-22 September 1994. Aust. Natl. Comm. Int. Dairy Fed., Glen Iris, Victoria, Australia.
    • (1994) Brief Commun. XXIV Int. Dairy Congr. , pp. 207
    • Jakob, E.1    Sievert, C.2    Puhan, Z.3
  • 21
    • 0028838504 scopus 로고
    • Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor
    • Kemmink, J., and T. E. Creighton. 1995. Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor. Biochemistry 34:12630-12635.
    • (1995) Biochemistry , vol.34 , pp. 12630-12635
    • Kemmink, J.1    Creighton, T.E.2
  • 22
    • 0026216795 scopus 로고
    • Three-dimensional molecular modeling of bovine caseins: κ-casein
    • Kumosinski, T. F., E. M. Brown, and H. M. Farrell, Jr. 1991. Three-dimensional molecular modeling of bovine caseins: κ-casein. J. Dairy Sci. 74:2879-2887.
    • (1991) J. Dairy Sci. , vol.74 , pp. 2879-2887
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell H.M., Jr.3
  • 23
    • 0027661562 scopus 로고
    • Three-dimensional molecular modeling of bovine caseins: A refined, energy-minimized κ-casein structure
    • Kumosinski, T. F., E. M. Brown, and H. M. Farrell, Jr. 1993. Three-dimensional molecular modeling of bovine caseins: a refined, energy-minimized κ-casein structure. J. Dairy Sci. 76: 2507-2520.
    • (1993) J. Dairy Sci. , vol.76 , pp. 2507-2520
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell H.M., Jr.3
  • 24
    • 0018133968 scopus 로고
    • Prediction of the conformation of the cow and sheep κ-caseins
    • Loucheux-Lefebvre, M.-H., J.-P. Aubert, and P. Jollès. 1978. Prediction of the conformation of the cow and sheep κ-caseins. Biophys. J. 23:323-336.
    • (1978) Biophys. J. , vol.23 , pp. 323-336
    • Loucheux-Lefebvre, M.-H.1    Aubert, J.-P.2    Jollès, P.3
  • 25
    • 0023096760 scopus 로고
    • Comparison of conformations of κ-casein, para-κ-casein and glycomacropeptide
    • Ono, T., R. Yada, K. Yutani, and S. Nakai. 1987. Comparison of conformations of κ-casein, para-κ-casein and glycomacropeptide. Biochim. Biophys. Acta 911:318-325.
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 318-325
    • Ono, T.1    Yada, R.2    Yutani, K.3    Nakai, S.4
  • 26
    • 0029352134 scopus 로고
    • Restrained molecular dynamics study of the interaction between bovine κ-casein peptide 98-111 and bovine chymosin and porcine pepsin
    • Plowman, J. E., and L. K. Creamer. 1995. Restrained molecular dynamics study of the interaction between bovine κ-casein peptide 98-111 and bovine chymosin and porcine pepsin. J. Dairy Res. 62:451-467.
    • (1995) J. Dairy Res. , vol.62 , pp. 451-467
    • Plowman, J.E.1    Creamer, L.K.2
  • 28
    • 85030056560 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 29
    • 0031415462 scopus 로고    scopus 로고
    • Restrained molecular dynamics investigation of the differences in association of chymosin to κ-caseins A and C
    • Plowman, J. E., L. K. Creamer, M. H. Smith, and J. P. Hill. 1997. Restrained molecular dynamics investigation of the differences in association of chymosin to κ-caseins A and C. J. Dairy Res. 64:299-304.
    • (1997) J. Dairy Res. , vol.64 , pp. 299-304
    • Plowman, J.E.1    Creamer, L.K.2    Smith, M.H.3    Hill, J.P.4
  • 30
    • 84989011989 scopus 로고
    • Proton assignment and structural features of a peptide from the chymosin-sensitive region of bovine κ-casein determined by 2D-NMR spectroscopy
    • Plowman, J. E., M. H. Smith, L. K. Creamer, M. J. Liddell, J. M. Coddington, J. J. Gibson, and D. R. Engelbretsen. 1994. Proton assignment and structural features of a peptide from the chymosin-sensitive region of bovine κ-casein determined by 2D-NMR spectroscopy. Magn. Reson. Chem. 32:458-464.
    • (1994) Magn. Reson. Chem. , vol.32 , pp. 458-464
    • Plowman, J.E.1    Smith, M.H.2    Creamer, L.K.3    Liddell, M.J.4    Coddington, J.M.5    Gibson, J.J.6    Engelbretsen, D.R.7
  • 31
    • 0020595601 scopus 로고
    • Peptide substrates for chymosin (rennin): Conformational studies of κ-casein and some κ-casein-related oligopeptides by circular dichroism and secondary structure prediction
    • Raap, J., K.E.T. Kerling, H. J. Vreeman, and S. Visser. 1983. Peptide substrates for chymosin (rennin): conformational studies of κ-casein and some κ-casein-related oligopeptides by circular dichroism and secondary structure prediction. Arch. Biochem. Biophys. 221:117-124.
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 117-124
    • Raap, J.1    Kerling, K.E.T.2    Vreeman, H.J.3    Visser, S.4
  • 32
    • 0344739060 scopus 로고    scopus 로고
    • Towards understanding the variant effect on the rate of cleavage by chymosin on κ-caseins A and C
    • Int. Dairy Fed. Int. Dairy Fed., Brussels, Belgium
    • Smith, M. H., J. P. Hill, L. K. Creamer, and J. E. Plowman, 1998. Towards understanding the variant effect on the rate of cleavage by chymosin on κ-caseins A and C. Pages 185-188 in Milk Protein Polymorphism. Int. Dairy Fed. Special Issue 9702. Int. Dairy Fed., Brussels, Belgium.
    • (1998) Milk Protein Polymorphism , Issue.9702 SPEC. ISSUE , pp. 185-188
    • Smith, M.H.1    Hill, J.P.2    Creamer, L.K.3    Plowman, J.E.4
  • 34
    • 0017349781 scopus 로고
    • Peptide substrates for chymosin (rennin). Kinetic studies with bovine κ-casein-(103-108)-hexapeptide analoges
    • Visser, S., P. J. van Rooijen, C. Schattenkerk, and K.E.T. Kerlíng. 1977. Peptide substrates for chymosin (rennin). Kinetic studies with bovine κ-casein-(103-108)-hexapeptide analoges. Biochim. Biophys. Acta 481:171-176.
    • (1977) Biochim. Biophys. Acta , vol.481 , pp. 171-176
    • Visser, S.1    Van Rooijen, P.J.2    Schattenkerk, C.3    Kerlíng, K.E.T.4
  • 35
    • 0028533901 scopus 로고
    • Secondary structures in β-casein peptide 1-42: A two dimensional nuclear magnetic resonance study
    • Wahlgren, N. M., P. Djemek, and T. Drakenberg 1994. Secondary structures in β-casein peptide 1-42: a two dimensional nuclear magnetic resonance study. J. Dairy Res. 61:495-506.
    • (1994) J. Dairy Res. , vol.61 , pp. 495-506
    • Wahlgren, N.M.1    Djemek, P.2    Drakenberg, T.3
  • 36
    • 85025797643 scopus 로고
    • On the stability of casein micelles
    • Walstra, P. 1990. On the stability of casein micelles. J. Dairy Sci. 73:1965-1979.
    • (1990) J. Dairy Sci. , vol.73 , pp. 1965-1979
    • Walstra, P.1
  • 38
    • 38249018583 scopus 로고
    • How to obtain accurate CAMELSPIN or ROESY spectra with identical low-power pulses for both the preparation and the mixing intervals
    • Zagorski, M. G. 1990. How to obtain accurate CAMELSPIN or ROESY spectra with identical low-power pulses for both the preparation and the mixing intervals. J. Magn. Reson 89: 608-614.
    • (1990) J. Magn. Reson , vol.89 , pp. 608-614
    • Zagorski, M.G.1


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