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A model for the assembly of bovine casein micelles from F2 and F3 subunits

Published online by Cambridge University Press:  01 June 2009

Tomotada Ono  and
Takayuki Obata
Tomotada Ono
Affiliation:
Department of Agricultural Chemistry, Iwate University, Morioka, Iwate 020, Japan
Takayuki Obata
Affiliation:
Department of Agricultural Chemistry, Iwate University, Morioka, Iwate 020, Japan
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Summary

Casein micelles were reassembled from mixtures of F2 and F3 subunits, the major subunits of bovine casein micelles, in varying ratios. The average radius of the reassembled micelles was inversely proportional to the F2 content. Based on this relationship, a model for casein micelle assembly is proposed in which the F3 subunit forms the core of the micelle with F2 subunit occurring on the surface. Micelle size can subsequently be defined by the F2 content.

Type
Original Articles
Information
Journal of Dairy Research , Volume 56 , Issue 3: Special Issue: Proceedings of the Hannah Research Institute Casein Conference , May 1989 , pp. 453 - 461
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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References

REFERENCES

Aoki, T., Kako, Y. & Imamuka, T. 1980 Separation of casein aggregates cross-linked by colloidal calcium phosphate from bovine casein micelles by high performance gel chromatography in the presence of urea. Journal of Dairy Research 53 53–59Google Scholar
Aschaffenburg, R. 1963 Preparation of βcasein by a modified urea fractionution method. Journal of Dairy Research 30 259–201CrossRefGoogle Scholar
Britten, M., Boulet, M. & Paquin, P. 1986 Composition and interfacial properties of casein micelle fractions. Journal of Dairy Research 53 573–584Google Scholar
Buchheim, W. & Welsch, U. 1973 Evidence for the submicellar composition of casein micelles on the basis of electron microscopical studies. Netherlands Milk and Dairy Journal 27 163–180Google Scholar
Clarke, R. & Nakai, S. 1971 Investigation of κ-αs1-casein interaction by fluorescence polarisation. Biochemistry 10 3353–3357Google Scholar
Fox, P. F. & Guiney, J. 1972 A procedure for the partial fractionation of the αs - and κ-caseins. Journal of Dairy Research 39 49–53Google Scholar
Gornali, A. G., Bardwill, C. S. & David, M. M. 1949 Determination of serum proteins by means of the Biuret reaction. Journal of Biological Chemistry 177 751–766Google Scholar
Heller, W., Bhatnagar, H. L. & Nakagaki, M. 1962 Theoretical investigations on the light scattering of spheres. XII1. The wavelength exponent of differential turbidity spectra. Journal of Chemical Physics 36 1103–1170CrossRefGoogle Scholar
Holt, C., Parker, T. G. & Dalgleish, D. G. 1975 Measurement of particle sizes by elastic and quasi-elastic light scattering. Biochimica et Biophysica Acta 400 283–292Google Scholar
Kaminogawa, S., Dosako, S. & Yamauchi, K. 1974 Studies on molecular properties of αs1-κ-casein complex by the hydrodynamical methods. Agricultural and Biological Chemistry 38 2337–2341Google Scholar
Kudo, S. & Mada, M. 1983 Interactions between αs2-casein and κ--casein as determined by gel filtration. New Zealand Journal of Dairy Science, and Technology 18 225–232Google Scholar
Levenberg, K. 1944 A method for the solution of certain non-linear problems in least squares. Quarterly Applied Mathematics 12 164–168Google Scholar
Melachouris, N. 1969 Discontinuous gel electrophoresis of whey proteins, casein and clotting enzymes. Journal of Dairy Science 52 456–459CrossRefGoogle ScholarPubMed
Obata, T. 1988 The structure and properties of casein micelles. Master Thesis of Agriculture. Department of Agricultural Chemistry, Iwate University, JapanGoogle Scholar
Ono, T., Furuyama, T. & Odagiri, S. 1983 a Formation of artificial casein micelles. Agricultural and Biological Chemistry 47 221–226Google Scholar
Ono, T., Odagiri, S. & Takagi, T. 1983 b Separation of the submicelles from micellar casein by high performance gel chromatography on a TSK-GEL G4000SW column. Journal of Dairy Research 50 37–44Google Scholar
Ono, T. & Takagi, T. 1986 Molecular weights of subunit components of bovine casein micelles. Journal of Dairy Research 53 547–555Google Scholar
Payens, T. A. J. & Nijhuis, H. 1974 Electrophoresis of interacting proteins. 1. Complex formation of αs1- and β-casein. Biochimica et Biophysica Acta 336 201–212Google Scholar
Schmidt, D. G. & Buchheim, W. 1970 [An electron-microscopic investigation of the substructure of the casein micelles in cow's milk]. Milchwissenschaft 25 596–600Google Scholar
Schmidt, D. G. & Payens, T. A. J. 1976 Micellar aspects of casein. Surface and Colloid Science 9 165–229Google Scholar
Schmidt, D. G. 1982 In Developments in Dairy Chemistry–1, pp. 61–86 (Ed. Fox, P. F.). London: Applied Science PublishersGoogle Scholar
Slattery, C. W. & Evard, R. 1973 A model for the formation and structure of casein micelles from subunits of variable composition. Biochimica et Biophysica Acta 317 529–538Google Scholar
Swaisgood, H. E. 1982 In Developments in Dairy Chemistry – 1 pp. 1–59 (Ed. Fox, P. F.) London: Applied Science PublishersGoogle Scholar
Talbot, B. & Waugh, D. F. 1970 Micelle-forming characteristics of monomeric and covalent polymeric κ- caseins. Biochemistry 9 2807–2813CrossRefGoogle ScholarPubMed
Waugh, D. F., Creamer, L. K., Slattery, C. W. & Dresdner, G. W. 1970 Core polymers of casein micelles. Biochemistry 9 786–795Google Scholar
Yoshikawa, M., Sugimoto, E. & Chiba, H. 1975 Studies on the interaction between αs1- and β-caseins. Agricultural and Biological Chemistry 39 1843–1849Google Scholar
Zittle, C. A. & Custer, J. H. 1963 Purification and some of the properties of αs-casein and κ-casein. Journal of Dairy Science 46 1183–1188Google Scholar