Characterization, kinetics and comparative properties of thiol:protein disulfide oxidoreductase

摘要: Abstract An enzyme capable of catalyzing thiol:protein disulfide exchange with glutathione and insulin has been purified to apparent homogeneity as judged by disc electrophoresis, electrophoresis sodium dodecyl sulfate, equilibrium ultracentrifugation amino acid sequence analysis the glycoprotein. The isoelectric point 4.10 other physicochemical properties are somewhat different from those similar enzymes described investigators, although there similarities in substrate specificity kinetic parameters. solubilized catalyzes interchange well a variety thiol-containing compounds. Although is best protein tested, vasopressin, oxytocin, ribonuclease also utilized. In presence glutathione, restoration active conformation “scrambled” ribonuclease. Catalysis depends on an cysteine residue which can be alkylated/inactivated only