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牛源SH-κ-酪蛋白的一些缔合特性

Some association properties of bovine SH-kappa-casein.

作者信息

Vreeman H J, Brinkhuis J A, van der Spek C A

出版信息

Biophys Chem. 1981 Oct;14(2):185-93. doi: 10.1016/0301-4622(81)85018-1.

Abstract

(1) It is shown that kappa-casein association is characterized by a critical micelle concentration which decreases as the ionic strength is increased. (2) The kappa-casein polymer molecular weight was calculated from the weight-average apparent molecular weight by taking into consideration the monomer concentration and the excluded volume. The degree of polymerization is 30 and does not depend on ionic strength between 0.1 and 1 M. (3) The non-electrical contribution to the standard free energy of association is -38 kJ/mol monomer. The electrical part is small: 1-2 kJ/mol monomer depending on the ionic strength and kappa-casein genetic variant. (4) The limitation of size and the size itself of the kappa-casein polymer can be explained by the theory of self-assembly of virus particles by Caspar and Klug (D.L.D. Caspar and A. Klug, Cold Spring Harb. Symp. Quant. Biol. 27 (1962)1). (5) Extending this theory to casein micelle assembly, it is predicted that micelles are distributed preferentially over a restricted number of sizes.

摘要

(1) 研究表明,κ-酪蛋白缔合的特征在于存在一个临界胶束浓度,该浓度会随着离子强度的增加而降低。(2) 通过考虑单体浓度和排除体积,由重均表观分子量计算出κ-酪蛋白聚合物的分子量。聚合度为30,且在0.1至1 M的离子强度范围内不依赖于离子强度。(3) 缔合标准自由能的非电贡献为-38 kJ/mol单体。电部分较小:取决于离子强度和κ-酪蛋白遗传变体,为1 - 2 kJ/mol单体。(4) κ-酪蛋白聚合物的尺寸限制及其本身的尺寸可以用卡斯帕和克鲁格提出的病毒颗粒自组装理论来解释(D.L.D.卡斯帕和A.克鲁格,《定量生物学冷泉港研讨会》27 (1962)1)。(5) 将该理论扩展到酪蛋白胶束组装,预计胶束优先分布在有限数量的尺寸上。

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