title: The nature of the multiple forms of bovine thiol:protein disulfide oxidoreductase.
abstract: Preparations of thiol"protein disulfide oxidoreductase from bovine liver were shown to be homogeneous by polyacrylamide gel electrophoresis, sedimentation equilibrium centrifugation and NH2-terminal analysis (Carmichael et al., 1977). When the enzyme was subjected to prolonged storage at -20 degrees, freeze-thawing, or heating at 60 degrees, at least one new protein species was observed using polyacrylamide gel electrophoresis. The new protein results from dimerization of the enzyme. The dmier consisted of two monomers held together by an intermolecular disulfide bond. The formation of this dimer can be reversed and partially prevented by thiols.
mesh_terms: D000818:Animals; D002417:Cattle; D002498:Centrifugation; D004591:Electrophoresis, Polyacrylamide Gel; D005615:Freezing; D006358:Hot Temperature; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione); D013997:Time Factors
chemical_list: D046911:Macromolecular Substances; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione)