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Structure of the casein micelle. The accessibility of the subunits to various reagents

Published online by Cambridge University Press:  01 June 2009

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

Carboxypeptidase A (CPA, mol. wt = 34600) and 1-dimethylaminonaphthalene-5-sulphonyl chloride (dansyl chloride, mol. wt = 270) were shown to react with the 3 casein subunits, αs1-, β- and κ-caseins, which constitute the micelle. Virtually all of the C-terminal amino acids were released by CPA from these subunits without disrupting the micellar structure.

It was verified that the rate of dissociation of the micelle into low molecular weight complexes is considerably slower than the rates at which these reagents act on micellar components. It is concluded that dansyl chloride, CPA, and probably also rennin, whose molecular weight is similar to that of CPA, are able to penetrate to the interior of the micelles. This was confirmed in a quite independent way with a non-reacting agent, myoglobin (mol. wt = 17000).

It is postulated that the casein micelle has a sponge-like structure in which the 3 different subunits are distributed fairly uniformly.

Micellar fractions obtained by differential centrifugation from skim-milk and colostrum were examined for their content of αs1-, β-, κ- and para-κ-caseins by the use of CPA as described by Ribadeau Dumas (1968). The results confirm that there is a real difference in κ-casein content of the micelles, according to their rate of sedimentation.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 2 , June 1970 , pp. 269 - 278
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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References

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