[Isolation and certain properties of mutant alkaline phosphatase of Escherichia coli].

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Article

[Isolation and certain properties of mutant alkaline phosphatase of Escherichia coli].

Biokhimiia (Moscow, Russia) - 1 Jan 1996

Nesmeianova M A, Krupianko V I, Kalinin A E, Kadyrova L Iu

Abstract excerpt

Natural and mutant alkaline phosphatases with amino acid substitutions in the processing site and N-terminal domain of the mature polypeptide chain Val for Ala(-1), Gln for Glu (+4) and simultaneously Gln for Glu (+4) and Ala for Arg (+1) have been isolated from the periplasm and cultural fluid of E. coli. It has been found that these substitutions have little effect on the dependence of the enzyme activity on...

Topics

Alkaline Phosphatase
Amino Acid Sequence
Catalysis
Escherichia coli
Hydrogen-Ion Concentration
Hydrolysis
Isoenzymes
Kinetics
Molecular Sequence Data
Mutation
Osmolar Concentration
Temperature

Source

Open in PubMed

Identifiers

PMID: 8679783

Provenance

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