Abstract
1) Thiamine monophosphate kinase absolutely required a certain monovalent cation, especially K+, for activity. 2) Enzyme activity was inhibited by ATP at high concentrations, and the inhibition was found to be due to a certain degree to the chelating action of Mg++. 3) Enzyme activity was scarcely affected by the intracellular concentration of thiamine pyrophosphate. © 1973, Center for Academic Publications Japan. All rights reserved.
Cite
CITATION STYLE
Nishino, H., Iwashima, A., & Nose, Y. (1973). Biogenesis of cocarboxylase in escherichia coli: Regulatory properties of thiamine monophosphate kinase. Journal of Nutritional Science and Vitaminology, 19(6), 505–511. https://doi.org/10.3177/jnsv.19.505
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.