Further characterization of the two catalases in Escherichia coli

Efrat Meir; Ezra Yagil

doi:10.1007/BF01567889

Further characterization of the two catalases in Escherichia coli

Efrat Meir
, Ezra Yagil^*

^*Corresponding author for this work

Biochemistry Molecular Biology

Tel Aviv University

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

Crude extracts of wild-type Escherichia coli contain two catalase species that separate on native polyacrylamide gels. The slow-migrating enzyme (HPII) has two pH optima of activity (at pH 6.8 and 10.5), is activated at 70°C, is sensitive to inhibitory by 3-amino-1,2,4-triazole and has Km values of 18.2 m M at pH 6.8 and of 10 m M at pH 10.5. The fast-migrating enzyme has a single pH optimum of 6.8 and is composed of two isozymes (HPI-A and HPI-B). Its activity is labile at 70°C, it is relatively resistant to inhibition by 3-amino-1,2,4-triazole and has a Km value of 3.7 m M.

Original language	English
Pages (from-to)	315-319
Number of pages	5
Journal	Current Microbiology
Volume	12
Issue number	6
DOIs	https://doi.org/10.1007/BF01567889
State	Published - Nov 1985

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title = "Further characterization of the two catalases in Escherichia coli",

abstract = "Crude extracts of wild-type Escherichia coli contain two catalase species that separate on native polyacrylamide gels. The slow-migrating enzyme (HPII) has two pH optima of activity (at pH 6.8 and 10.5), is activated at 70°C, is sensitive to inhibitory by 3-amino-1,2,4-triazole and has Km values of 18.2 m M at pH 6.8 and of 10 m M at pH 10.5. The fast-migrating enzyme has a single pH optimum of 6.8 and is composed of two isozymes (HPI-A and HPI-B). Its activity is labile at 70°C, it is relatively resistant to inhibition by 3-amino-1,2,4-triazole and has a Km value of 3.7 m M.",

author = "Efrat Meir and Ezra Yagil",

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AB - Crude extracts of wild-type Escherichia coli contain two catalase species that separate on native polyacrylamide gels. The slow-migrating enzyme (HPII) has two pH optima of activity (at pH 6.8 and 10.5), is activated at 70°C, is sensitive to inhibitory by 3-amino-1,2,4-triazole and has Km values of 18.2 m M at pH 6.8 and of 10 m M at pH 10.5. The fast-migrating enzyme has a single pH optimum of 6.8 and is composed of two isozymes (HPI-A and HPI-B). Its activity is labile at 70°C, it is relatively resistant to inhibition by 3-amino-1,2,4-triazole and has a Km value of 3.7 m M.

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Further characterization of the two catalases in Escherichia coli

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