NADP+-isocitrat-dehydrogenase aus Idus idus (Pisces: Cyprinidae). II. Einfluß der temperatur auf substrat- und cosubstrataffinität |
| |
Authors: | Dr. H. Künnemann D. Passia |
| |
Affiliation: | (1) Present address: Lehrstuhl für Vergleichende Physiologie und Tierpsychologie, Zoologisches Institut der Universität Kiel, Kiel, Germany (FRG) |
| |
Abstract: | Maximum substrate and cosubstrate affinity, as judged by the Michaelis constant (KM), of NADP+-dependent isocitrate dehydrogenase of pig heart (purchased from Boehringer, Mannheim, FRG) is attained at 37°C. If KM-values of substrate (Isocitrate, IC) and cosubstrate (NADP+) of NADP+-dependent isocitrate dehydrogenase (ICDH) of the white dorsal muscle of Idus idus L. is plotted against the experimental temperature (VT), W-shaped curves result. With increasing adaptation temperature (AT), there is a shift to increasing VT. It is suggested that the W-shaped curves are due either to the simultaneous presence of two multiple forms of the enzyme, or to the reversible temperature-dependent interconversion of one protein species. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|