期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1973
卷号：19
期号：4
页码：339-347
DOI：10.3177/jnsv.19.339
出版社：Center for Academic Publications Japan
摘要：Pyridoxal 5'-phosphate (PLP), in high concentrations, was found to bind to lysine residues at non-catalytic sites of mammalian aspartate aminotransferase (GOT) and E. coil tryptophanase. This excess bind-ing of PLP caused significant decreases in the activities of these enzymes. The concentrations of PLP required for the 50% inhibition of GOT and tryptophanase were 2.5mM and 6.3mM, respectively. Pyridoxal (PL) also combined with these enzymes by forming SCHIFF's bases with lysine residues at the catalytic as well as non-catalytic sites. The concentration of PL necessary for the 50% inhibition of GOT activity was 5mM, indicating that the inhibitory action of PL is lower than that of PLP.
