COMPATIBLE SOLUTES AND INVITRO STABILITY OF SALSOLA-SODA ENZYMES - PROLINE INCOMPATIBILITY

被引：58

作者：

NIKOLOPOULOS, D

MANETAS, Y

机构：

[1] Laboratory of Plant Physiology, Department of Biology, University of Patras, Patras

来源：

PHYTOCHEMISTRY | 1991年 / 30卷 / 02期

关键词：

SALSOLA-SODA; CHENOPODIACEAE; COMPATIBLE SOLUTES; MALATE DEHYDROGENASE; NITRATE REDUCTASE; PHOSPHOENOLPYRUVATE CARBOXYLASE;

D O I：

10.1016/0031-9422(91)83694-G

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：

Proline is not compatible with enzymes extracted from Salsola soda, a glycine-betaine former adapted to saline soils. Proline accelerated thermal inactivation of nitrate reductase (EC 1.6.6.1), afforded no protection against dilution-induced inactivation of phosphoenolpyruvate carboxylase (EC 4.1.1.31) and only slightly opposed heat denaturation of NADH-dependent malate dehydrogenase (EC 1.1.1.37). Glycinebetaine, sorbitol and glycerol were, however, fully compatible, counteracting completely the adverse effects of heat and dilution. A co-evolution of enzyme structure and osmolyte systems, at least at the species level, is inferred from our results.

引用

页码：411 / 413

页数：3

共 25 条

[1] REVERSIBLE COLD INACTIVATION OF C-4 PHOSPHOENOLPYRUVATE CARBOXYLASE - FACTORS AFFECTING REACTIVATION AND STABILITY [J].