[Choice of a spin label probe in order to study the recombination of beta-hydroxybutyrate dehydrogenase of a rat liver inner mitochondrial membrane with lecithin vesicles].
We find from studying the inhibitory effect of N-ethylmaleimide (NEM) on the enzymatic activity of beta-hydroxybutyrate dehydrogenase, that approximately one molecule of NEM is bound for one molecule of protein when the enzymatic activity is completely inhibited. Since the protein is a dimer this implies that each molecule of protein possesses only one thiol group in its catalytic center. Two long chain maleimide derivates: (10.3) NEM and (1.14) NEM conform, if a reasonable assumption is accepted to the conditions required for the study of the recombination of beta-hydroxybutyrate dehydrogenase with lecithin vesicles by spin label technique.
D000818:Animals; D001665:Binding Sites; D004578:Electron Spin Resonance Spectroscopy; D005033:Ethylmaleimide / Q000494:pharmacology; D006884:Hydroxybutyrate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007460:Iodoacetamide / Q000494:pharmacology; D008301:Maleimides / Q000138:chemical synthesis / Q000494:pharmacology; D008930:Mitochondria, Liver / Q000201:enzymology*; D010713:Phosphatidylcholines / Q000378:metabolism*; D051381:Rats; D013113:Spin Labels / Q000138:chemical synthesis
D008301:Maleimides; D010713:Phosphatidylcholines; D013113:Spin Labels; D006884:Hydroxybutyrate Dehydrogenase; D005033:Ethylmaleimide; D007460:Iodoacetamide
Choix d'un marqueur de spin en vue d'étudier la recombinaison de la beta-hydroxybutyrate deshydrogenase de la membrane interne des mitochondries avec des vesicules de lécithine.