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Volumn 85, Issue 11, 2002, Pages 2711-2721

Casein interactions studied by the surface plasmon resonance technique

Author keywords

BIACORE; Bovine casein; Casein interaction; Surface plasmon resonance

Indexed keywords

BOVINAE;

EID: 0036835910     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(02)74358-0     Document Type: Article
Times cited : (46)

References (30)
  • 2
    • 0023667802 scopus 로고
    • Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate
    • Aoki, T., N. Yamada, I. Tomita, Y. Kako, and T. Imamura. 1987. Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate. Biochim. Biophys. Acta 911:238-243.
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 238-243
    • Aoki, T.1    Yamada, N.2    Tomita, I.3    Kako, Y.4    Imamura, T.5
  • 4
    • 0016757543 scopus 로고
    • The association of bovine β-casein. The importance of the C-terminal region
    • Berry, G. P., and L. K. Creamer. 1975. The association of bovine β-casein. The importance of the C-terminal region. Biochemistry. 14:3542-3545.
    • (1975) Biochemistry , vol.14 , pp. 3542-3545
    • Berry, G.P.1    Creamer, L.K.2
  • 5
    • 0002282109 scopus 로고
    • Forces involved in the enzymatic and the acidic coagulation of casein micelles
    • B. J. F. Hudson, ed., Elsevier Applied Sciences, London, United Kingdom
    • Bringe, N. A., and J. E. Kinsella. 1987. Forces involved in the enzymatic and the acidic coagulation of casein micelles. Pages 159-194 in Development in Food Protein. B. J. F. Hudson, ed., Elsevier Applied Sciences, London, United Kingdom.
    • (1987) Development in Food Protein , pp. 159-194
    • Bringe, N.A.1    Kinsella, J.E.2
  • 6
    • 0018461464 scopus 로고
    • On the size of monomers and polymers of β-casein
    • Buchheim, W., and D. G. Schmidt. 1979. On the size of monomers and polymers of β-casein. J. Dairy Res. 46:277-280.
    • (1979) J. Dairy Res. , vol.46 , pp. 277-280
    • Buchheim, W.1    Schmidt, D.G.2
  • 7
    • 0000942193 scopus 로고
    • Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein
    • Byler, D. M., and H. M. Farrel Jr. 1989. Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein. J. Dairy Sci. 72:1719-1723.
    • (1989) J. Dairy Sci. , vol.72 , pp. 1719-1723
    • Byler, D.M.1    Farrel Jr., H.M.2
  • 8
    • 84971722091 scopus 로고
    • The content and composition of protein in creamery milks in southwest Scotland
    • Davies, D. T., and A. J. R. Law. 1980. The content and composition of protein in creamery milks in southwest Scotland. J. Dairy Res. 47:83-90.
    • (1980) J. Dairy Res. , vol.47 , pp. 83-90
    • Davies, D.T.1    Law, A.J.R.2
  • 9
    • 0032839313 scopus 로고    scopus 로고
    • Casein micelle interactions
    • De Kruif, C. G. 1999. Casein micelle interactions. Int. Dairy J. 9:183-188.
    • (1999) Int. Dairy J. , vol.9 , pp. 183-188
    • De Kruif, C.G.1
  • 10
    • 0003125344 scopus 로고
    • The milk protein system
    • P. F. Fox, ed., Elsevier Applied Sciences, London, United Kingdom
    • Fox, P. F. 1989. The milk protein system. Pages 1-53 in Developments in Dairy Chemistry. P. F. Fox, ed., Elsevier Applied Sciences, London, United Kingdom.
    • (1989) Developments in Dairy Chemistry , pp. 1-53
    • Fox, P.F.1
  • 11
    • 0004915244 scopus 로고    scopus 로고
    • Binding of cations to casein molecules: Importance of physicochemical conditions
    • Gaucheron, F., Y. Le Graet, E. Boyaval, and M. Piot. 1997. Binding of cations to casein molecules: importance of physicochemical conditions. Milchwissenschaft. 52:322-327.
    • (1997) Milchwissenschaft , vol.52 , pp. 322-327
    • Gaucheron, F.1    Le Graet, Y.2    Boyaval, E.3    Piot, M.4
  • 12
    • 0026552375 scopus 로고
    • Reexamination of the polymeric distributions of bovine κ-casein
    • Groves, M. L., H. J. Dower, and H. M. Farrell Jr. 1992. Reexamination of the polymeric distributions of bovine κ-casein. J. Protein Chem. 11:21-26.
    • (1992) J. Protein Chem. , vol.11 , pp. 21-26
    • Groves, M.L.1    Dower, H.J.2    Farrell Jr., H.M.3
  • 13
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakama, S., and A. Nakai. 1985. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J. Food Sci. 50:486-491.
    • (1985) J. Food Sci. , vol.50 , pp. 486-491
    • Hayakama, S.1    Nakai, A.2
  • 14
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure in dairy products
    • Horne, D. S. 1998. Casein interactions: casting light on the black boxes, the structure in dairy products. Int. Dairy J. 8:171-177.
    • (1998) Int. Dairy J. , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 16
    • 0342813129 scopus 로고    scopus 로고
    • Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors
    • Karlsson, R., and A. Fält. 1997. Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200:121-133.
    • (1997) J. Immunol. Methods , vol.200 , pp. 121-133
    • Karlsson, R.1    Fält, A.2
  • 17
    • 0001750488 scopus 로고
    • Determination of protein hydrophobicity using a sodium dodecyl sulfate binding method
    • Kato, A., T. Matsuda, N. Matsudomi, and K. Kobayashi. 1984. Determination of protein hydrophobicity using a sodium dodecyl sulfate binding method. J. Agric. Food Chem. 32:284-287.
    • (1984) J. Agric. Food Chem. , vol.32 , pp. 284-287
    • Kato, A.1    Matsuda, T.2    Matsudomi, N.3    Kobayashi, K.4
  • 18
    • 0013968213 scopus 로고
    • Association of caseins and their possible relation to structure of casein micelle
    • Payens, T. A. J. 1966. Association of caseins and their possible relation to structure of casein micelle. J. Dairy Sci. 49:1317-1324.
    • (1966) J. Dairy Sci. , vol.49 , pp. 1317-1324
    • Payens, T.A.J.1
  • 19
    • 0004233290 scopus 로고
    • Biosensor, ed. Pharmacia Biosensor AB Uppsala, Sweden
    • Pharmacia Biosensor, AB. 1994. in BIAapplications Handbook. Biosensor, ed. Pharmacia Biosensor AB Uppsala, Sweden.
    • (1994) BIAapplications Handbook
  • 20
    • 0000529133 scopus 로고
    • Casein association and micelle formation
    • P. F. Fox, ed., Elsevier Science Publishers., Barking, United Kingdom
    • Rollema, H. S. 1992. Casein association and micelle formation. Pages 111-140 in Advanced Dairy Chemistry P. F. Fox, ed., Elsevier Science Publishers., Barking, United Kingdom.
    • (1992) Advanced Dairy Chemistry , pp. 111-140
    • Rollema, H.S.1
  • 22
    • 0000799754 scopus 로고
    • Micellar aspects of casein
    • E. Matijevic, ed. John Wiley and Sons, New York, NY
    • Schmidt, D. G., and T. A. J. Payens. 1976. Micellar aspects of casein. Pages 165-229 in Surface and Colloid Science. Vol. 9. E. Matijevic, ed. John Wiley and Sons, New York, NY.
    • (1976) Surface and Colloid Science. , vol.9 , pp. 165-229
    • Schmidt, D.G.1    Payens, T.A.J.2
  • 23
    • 0002429127 scopus 로고
    • Association of caseins and casein micelle structure
    • P. F. Fox, ed., Elsevier Science Publishers, London, United Kingdom
    • Schmidt, D. G. 1982. Association of caseins and casein micelle structure. Pages 61-86 in Developments in Dairy Chemistry - 1. P. F. Fox, ed., Elsevier Science Publishers, London, United Kingdom.
    • (1982) Developments in Dairy Chemistry - 1 , pp. 61-86
    • Schmidt, D.G.1
  • 24
    • 0024305880 scopus 로고
    • Hydrophobic interactions in human casein micelle formation: β-casein aggregation
    • Slattery, C. W., S. M. Sood, and P. Chang. 1989. Hydrophobic interactions in human casein micelle formation: β-casein aggregation. J. Dairy Res. 56:427-433.
    • (1989) J. Dairy Res. , vol.56 , pp. 427-433
    • Slattery, C.W.1    Sood, S.M.2    Chang, P.3
  • 27
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • Elsevier Applied Science, London, United Kingdom
    • Swaisgood, H. E. 1992. Chemistry of the caseins. Pages 63-110 in Advanced Dairy Chemistry - 1: protein 2nd ed. Elsevier Applied Science, London, United Kingdom.
    • (1992) Advanced Dairy Chemistry - 1: Protein 2nd Ed. , pp. 63-110
    • Swaisgood, H.E.1
  • 28
    • 0027685785 scopus 로고
    • Review and update of casein chemistry
    • Swaisgood, H. E. 1993. Review and update of casein chemistry. J. Dairy Sci. 76:3054-3061.
    • (1993) J. Dairy Sci. , vol.76 , pp. 3054-3061
    • Swaisgood, H.E.1
  • 29
    • 0023399412 scopus 로고
    • Structure of casein micelle. I. Small angle neutron scattering and light scattering from β- and κ-casein
    • Thurn, A., W. Burchard, and R. Niki. 1987. Structure of casein micelle. I. Small angle neutron scattering and light scattering from β- and κ-casein. Colloids Polymer Sci. 265:653-666.
    • (1987) Colloids Polymer Sci. , vol.265 , pp. 653-666
    • Thurn, A.1    Burchard, W.2    Niki, R.3
  • 30
    • 85025797643 scopus 로고
    • On the stability of casein micelles
    • Walstra, P. 1990. On the stability of casein micelles. J. Dairy Sci. 73:1965-1977.
    • (1990) J. Dairy Sci. , vol.73 , pp. 1965-1977
    • Walstra, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.