Studies on the Metabolism of Borate. IV. Effect of Borate on Glyceraldehydephosphate Dehydrogenase.
- 1 January 1966
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 14 (5) , 467-473
- https://doi.org/10.1248/cpb.14.467
Abstract
Fructose 1, 6-diphosphate and fructose 6-monophosphate were accumulated by borate in anaerobic glycolysis system of liver homogenates of guinea pigs. Glyceraldehydephosphate dehydrogenase (GAP dehydrogenase) from yeast and in liver homogenates of guinea pigs and rats were found to be inhibited by borate. The inhibition was observed in both cases in which free D-glyceral-dehyde or D-glyceraldehyde 3-phosphate was used as substrate. GAP dehydrogenase was inhibited competitively by borate, and the inhibition was reversed by dialysis, but not reversed by excess sugars or poly-hydroxy compounds in the experimental condition. Borate has no effect on lactate dehydrogenase from rabbit muscle and also in liver homogenates of guinea pigs. Toxicity of borate was discussed from biochemical point of view.This publication has 1 reference indexed in Scilit:
- Reversible Direct Hydrogen Transfer from Reduced Pyridine Nucleotides to Cytochrome b5 ReductaseJournal of Biological Chemistry, 1964