ON TEMPERATURE DEPENDENCE OF CONFORMATION OF HUMAN SERUM HIGH DENSITY LIPOPROTEIN

被引：28

作者：

SCANU, AM

机构：

[1] Departments of Medicine and Biochemistry, University of Chicago, Argonne Cancer Research Hosp. Operated by the Univ. of Chicago for the U.S. Atomic Energy Commission, Chicago, IL

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 181卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0005-2795(69)90249-9

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：

1. 1. Human serum lipoprotein of d 1.063-1.125, HDL2 and its delipidated product, apo HDL2, were studied by the techniques of circular dichroism and ultraviolet spectroscopy as a function of temperature. 2. 2. The observed thermal transitions were greater in apo HDL2 than in HDL2. In both instances the changes were reversible, although the course of renaturation was slower in the products deprived of lipids. 3. 3. The results were taken to support the view that lipids play a structural role in HDL2 in that they pose constraints on the temperature dependent conformational instability of the protein. 4. 4. Sodium dodecyl sulphate at high concentrations (20-200 mM) had an effect on apo HDL2 similar to that of lipids. © 1969.

引用

页码：268 / &

共 17 条

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