Enzyme activities in concentrated solutions of glycinebetaine and other solutes
β Scribed by A. Pollard; R. G. Wyn Jones
- Publisher
- Springer-Verlag
- Year
- 1979
- Tongue
- English
- Weight
- 755 KB
- Volume
- 144
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
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.
π SIMILAR VOLUMES
## Γ Ε½ . Ε½ . 4 components of x 2.8LiCl q LiNO q 1 y x H O , no experimental data on this ternary 3 2 system are utilized. This fact underlies the predictive quality of the theoretical model Ε½ presented in our paper. By induction, we extend our results to the case of water q N . electrolytes .