DETERMINATION OF BINDING AFFINITIES OF GLUCOSE-OXIDASE FOR SODIUM N-DODECYL SULFATE

被引：24

作者：

HOUSAINDOKHT, MR ^{[1
]}

MOOSAVIMOVAHEDI, AA ^{[1
]}

机构：

[1] UNIV TEHRAN, DEPT BIOCHEM & BIOPHYS, TEHRAN, IRAN

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 1994年 / 16卷 / 02期

关键词：

SODIUM N-DODECYL SULFATE; GLUCOSE OXIDASE; BINDING AFFINITIES;

D O I：

10.1016/0141-8130(94)90018-3

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 binding of sodium n-dodecyl sulfate (SDS) to glucose oxidase was studied at pH 3.2 and 6.4 by equilibrium dialysis at 37 degrees C. The binding data have been analysed in terms of Scatchard plots which show unusual minima. These plots were analysed for two interacting sets of sites. Equations for the free energy of binding of each set of sites were obtained by a combination of the Tanford and Hill theories to obtain the affinities of each set of sites.

引用

页码：77 / 80

页数：4

共 14 条

[1]

HILL AV, 1910, J PHYSIOL-LONDON, V40, pP4

[2] BINDING OF NORMAL-ALKYL SULFATES TO LYSOZYME IN AQUEOUS-SOLUTION [J].