MICRO-CALORIMETRIC STUDY OF GLUTAMINE FIXATION ON THE GLUTAMINE-BINDING PROTEIN OF ESCHERICHIA-COLI

被引：9

作者：

MARTY, B

GAUDIN, C

RAGOT, M

BELAICH, A

BELAICH, JP

机构：

[1] Laboratoire de Chimie Bactérienne, C.N.R.S.

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 86卷 / 04期

关键词：

D O I：

10.1016/0006-291X(79)90233-X

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 enthalpy variation (ΔH) induced by addition of glutamine to glutamine binding protein isolated from E. coli has been studied by microcalorimetry. The reaction was very exothermic. The free energy variation (ΔG) was calculated from the dissociation constant (KD) measured by dialysis techniques. The entropic variation (ΔS) was deduced from ΔG and ΔH values; it was found highly negative, indicating that an important conformational change is occuring. Comparison with others binding proteins and possible significance of such a phenomenon is discussed. © 1979.

引用

页码：1118 / 1125

页数：8

共 23 条

[1] TRANSPORT OF SUGARS AND AMINO-ACIDS IN BACTERIA .17. EXISTENCE AND NATURE OF SUBSTRATE AMINO-ACIDS BOUND TO PURIFIED BRANCHED-CHAIN AMINO ACID-BINDING PROTEINS OF ESCHERICHIA-COLI [J].