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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus subtilis / enzymology*
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Bacillus subtilis / genetics
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Protein Denaturation
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Protein Multimerization
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Protein Refolding
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Protein Subunits / chemistry*
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Protein Subunits / genetics
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Protein Subunits / metabolism
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Species Specificity
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Temperature
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gamma-Glutamyltransferase / chemistry*
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gamma-Glutamyltransferase / genetics
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gamma-Glutamyltransferase / metabolism
Substances
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Bacterial Proteins
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Protein Subunits
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gamma-Glutamyltransferase