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Structure of the casein micelle. A proposed model

Published online by Cambridge University Press:  01 June 2009

J. Garnier  and
B. Ribadeau Dumas
J. Garnier
Affiliation:
Laboratoire de Recherches sur les Protéines, Département de Technologie animale, I. N. R. A., 78, Jouy-en-Josas, France
B. Ribadeau Dumas
Affiliation:
Laboratoire de Recherches sur les Protéines, Département de Technologie animale, I. N. R. A., 78, Jouy-en-Josas, France
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Summary

On the basis of complete permeability by high molecular weight reagents of casein micelles in milk and a uniform distribution of the 3 different casein subunits, a model of the micelle structure is proposed. It is composed of an average repeating unit of 1 κ-, 2 αs1;- and β-casein subunits assembled in a 3-dimensional network or branched polymer made of 130–130000 monomers, in which the trimers of κ-casein occupy the nodes and the copolymers of αs1;- and β-caseins make up the branches. All the associations between subunits are through non-covalent bonds. The chemical composition varies with the number of αs1;- and β;-casein subunits in the branches. This proposed structure is strongly supported by evidence from electron microscopy and a scale model has been made. It leads to an understanding of the role of κ-casein in micelle formation and opens new perspectives in explaining some properties of the caseins. It offers an interesting example of a new type of quaternary structure of protein subunits.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 3 , October 1970 , pp. 493 - 505
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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