title: Thermal denaturation and renaturation of γ-glutamyltranspeptidase of Escherichia coli.
abstract: Heat-treated γ-glutamyltranspeptidase of Escherichia coli recovered enzymatic activity after incubation at 4 °C, while heat-treated γ-glutamyltranspeptidase of Bacillus subtilis did not. Fluorescent spectra, CD spectra, and native polyacrylamide gel electrophoresis analysis suggested that the dimer of E. coli γ-glutamyltranspeptidase was separated into protomers by heat-treatment, but was renatured by incubation at 4 °C.
authors: Division of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Matsugasaki, Kyoto, Japan.
authors: Thao Van
authors: TV
authors: Ho
authors: Kaeko
authors: K
authors: Kamei
authors: Kei
authors: K
authors: Wada
authors: Keiichi
authors: K
authors: Fukuyama
authors: Hideyuki
authors: H
authors: Suzuki
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D011489:Protein Denaturation; D055503:Protein Multimerization; D058849:Protein Refolding; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013045:Species Specificity; D013696:Temperature; D005723:gamma-Glutamyltransferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; D005723:gamma-Glutamyltransferase