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- W3021545900 abstract "A high-level expression system for the Escherichia coli HB101 γ-glutamyltranspeptidase (GGT) gene was constructed to obtain a sufficient amount of the enzyme for structural studies. About 300 mg of the enzyme was purified from 2 1 of culture broth. Both subunits were needed to reconstitute GGT activity. The E. coli GGT and the Pseudomonas GGT were compared with respect to catalytic properties and immunological relationships. Enzymes showed different acceptor specificities. Relatively high immunocross-reactivity was observed between the small subunits of both enzymes by Western blot analysis using antibodies prepared agsinst either enzyme." @default.
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- W3021545900 date "1992-10-01" @default.
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- W3021545900 title "Bacterial γ-glutamyltranspeptidases: Comparison ofEscherichia coliandPseudomonasγ-glutamyltranspeptidase" @default.
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- W3021545900 doi "https://doi.org/10.1111/j.1574-6968.1992.tb05469.x" @default.
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