Department of Biochemistry and Soil Science, University College of North Wales, Deiniol Road, LL57 2UW, Bangor, Gwynedd, Wales, U.K..
Planta. 1979 Jan;144(3):291-8. doi: 10.1007/BF00388772.
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.
已研究了甘氨酸甜菜碱和其他溶质的浓缩溶液中许多酶的活性。与 NaCl 等电解质不同，甘氨酸甜菜碱在高达 500mM 时没有抑制作用。这与甘氨酸甜菜碱在细胞质渗透调节中的假定作用是一致的。在某些情况下，甘氨酸甜菜碱对 NaCl 抑制有部分保护作用。使用大麦（Hordeum vulgare）中的苹果酸脱氢酶（脱羧）进行了更详细的甘氨酸甜菜碱-NaCl-酶相互作用研究。
