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Micellar structure of beta-casein observed by small-angle X-ray scattering.

作者信息

Kajiwara K, Niki R, Urakawa H, Hiragi Y, Donkai N, Nagura M

机构信息

Institute for Chemical Research, Kyoto University, Uji, Japan.

出版信息

Biochim Biophys Acta. 1988 Jul 20;955(2):128-34. doi: 10.1016/0167-4838(88)90186-0.

DOI:10.1016/0167-4838(88)90186-0
PMID:3395618
Abstract

The small-angle X-ray scattering was observed from beta-casein micelles in 0.2 M phosphate buffer (pH 6.7) with varying temperatures. An oblate ellipsoid of a rigid core with a thin soft layer was proposed as a probable model of the beta-casein micellar structure, according to the results of the model optimization with simple triaxial bodies. Here the axial ratio was found to decrease and the micelle to become spherical when the polymerization proceeds with temperature. The consistency of the present model was examined with the results of hydrodynamic measurements published previously.

摘要

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