A 3-STATE HEAT-DENATURATION OF BOVINE ALPHA-LACTALBUMIN

被引：11

作者：

APENTEN, RKO

机构：

[1] Proctor, Department of Food Science, University of Leeds, Leeds, LS2 9JT, Woodhouse Lane

来源：

FOOD CHEMISTRY | 1995年 / 52卷 / 02期

关键词：

D O I：

10.1016/0308-8146(94)P4191-H

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The heat-denaturation of bovine alpha-lactalbumin (alpha-La) was studied using tryptophan and tyrosine fluorescence intensity measurements at 2-80 degrees C. The solvent used was sodium cacodylate buffer (10 mM, pH 6.0) with 1 mM EDTA or 9 mM CaCl2. The denaturation of apo-alpha-La conformed to a two-state reaction with a melting temperature (T-m) of 34.5 (+/- 0.7)degrees C. In contrast, the heat-unfolding of holo-alpha-La was consistent with a three-state reaction. The T-m for holo-alpha-La heat-unfolding was 47 (+/- 2.6)degrees C or 67.5 (+/- 1.3)degrees C as determined from tyrosine or tryptophan fluorescence changes, respectively. Such results suggest that Ca2+ binding preferentially stabilises one domain of alpha-La against heat-denaturation.

引用

页码：131 / 133

页数：3

共 22 条

[1]

ACHARYA KR, 1989, J MOL BIOL, V208, P27

[2] ALPHA-LACTALBUMIN - COMPACT STATE WITH FLUCTUATING TERTIARY STRUCTURE [J].