Studies on inosine monophosphate dehydrogenase. An associating-dissociating system.
The techniques of polyacrylamide gel electrophoresis, sedimentation velocity and frontal analysis on Sephadex have been used to demonstrate that preparations of IMP dehydrogenase (IMP: NAD+ oxidoreductase, EC 1.2.1.14) from Aerobacter aerogenes consist of a mixture of molecular weight isomers. Further, it has been shown that dissociation of the higher molecular weight forms is promoted by urea, sodium dodecyl sulphate and dithiothreitol. Under conditions comparable to those used for kinetic analyses, the enzyme has a molecular weight of about 86000 and this is the smallest active species that has been observed. In the absence of a reducing agent, the enzyme undergoes polymerization and is devoid of catalytic activity. From the amino acid composition and peptide map, it appears that the molecule with a molecular weight of 86000 is made up of two identical polypeptide chains.
D000596:Amino Acids / Q000032:analysis; D004229:Dithiothreitol / Q000494:pharmacology; D004754:Enterobacter / Q000201:enzymology; D007168:IMP Dehydrogenase / Q000378:metabolism*; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D014508:Urea / Q000494:pharmacology
D000596:Amino Acids; D046911:Macromolecular Substances; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol; D014508:Urea; D007168:IMP Dehydrogenase; D007658:Ketone Oxidoreductases; D004229:Dithiothreitol