MICELLAR STRUCTURE OF BETA-CASEIN OBSERVED BY SMALL-ANGLE X-RAY-SCATTERING

被引：36

作者：

KAJIWARA, K

NIKI, R

URAKAWA, H

HIRAGI, Y

DONKAI, N

NAGURA, M

机构：

[1] KYOTO UNIV, INST CHEM RES, UJI, KYOTO 611, JAPAN

[2] HOKKAIDO UNIV, FAC AGR, INST DAIRY SCI, SAPPORO, HOKKAIDO 060, JAPAN

[3] KYOTO INST TECHNOL, FAC ENGN & DESIGN, KYOTO 606, JAPAN

[4] SHINSHU UNIV, FAC TEXT RES, UEDA, JAPAN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1988年 / 955卷 / 02期

关键词：

D O I：

10.1016/0167-4838(88)90186-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 meauresments published previously.

引用

页码：128 / 134

页数：7

共 25 条

[1] CONFORMATION AND AGGREGATION OF BOVINE BETA-CASEIN-A .1. MOLECULAR ASPECTS OF THERMAL AGGREGATION [J].