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[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...

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PMID: 8679783

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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