ENZYME-ACTIVITIES IN CONCENTRATED-SOLUTIONS OF GLYCINEBETAINE AND OTHER SOLUTES

被引:320
作者
POLLARD, A
WYNJONES, RG
机构
[1] Department of Biochemistry and Soil Science, University College of North Wales, Bangor, LL57 2UW, Gwynedd, Deiniol Road
关键词
Electrolytes; Enzyme stability; Glycinebetaine; Hordeum; Malate dehydrogenase (decarboxylating);
D O I
10.1007/BF00388772
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The activities of a number of enzymes in concentrated solutions of glycinebetaine and other solutes have been studied. Glycinebetaine, in contrast to electrolytes such as NaCl, was found to be noninhibitory up to 500 mM. This is compatible with the postulated role of glycinebetaine in cytoplasmic osmoregulation. Partial protection against NaCl inhibition was afforded by glycinebetaine in some cases. More detailed studies on glycinebetaine -NaCl-enzyme interactions were carried out using malate dehydrogenase (decarboxylating) from Hordeum vulgare. © 1979 Springer-Verlag.
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页码:291 / 298
页数:8
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