Thermal Denaturation and Renaturation of γ-Glutamyltranspeptidase of Escherichia coli

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...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2013, Vol.77 (2), p.409-412
Hauptverfasser:	HO, Thao Van, KAMEI, Kaeko, WADA, Kei, FUKUYAMA, Keiichi, SUZUKI, Hideyuki
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus subtilis - enzymology Bacillus subtilis - genetics Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism denaturation Escherichia coli - enzymology Escherichia coli - genetics gamma-Glutamyltransferase - chemistry gamma-Glutamyltransferase - genetics gamma-Glutamyltransferase - metabolism Protein Denaturation Protein Multimerization Protein Refolding Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism renaturation Species Specificity Temperature γ-glutamyltranspeptidase
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Zusammenfassung:	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.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.120780