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Activation of a Mutationally Altered Form of the Escherichia Coli Alkaline Phosphatase by Zinc

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 1966 Jul 10
PMID 5330265
Citations 6
Authors
M J SCHLESINGER
Affiliations
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Citing Articles

Zinc-dependent conformational stability in the alkaline phosphatase of Escherichia coli.

Trotman C, Greenwood C Biochem J. 1969; 114(4):82P-83P.

PMID: 4981035 PMC: 1185041. DOI: 10.1042/bj1140082pb.

Effects of zinc and other metal ions on the stability and activity of Escherichia coli alkaline phosphatase.

Trotman C, Greenwood C Biochem J. 1971; 124(1):25-30.

PMID: 4942389 PMC: 1177109. DOI: 10.1042/bj1240025.

Mutationally altered rate constants in the mechanism of alkaline phosphatase.

Halford S, SCHLESINGER M Biochem J. 1974; 141(3):845-52.

PMID: 4618778 PMC: 1168190. DOI: 10.1042/bj1410845.

Localization of polyribosomes containing alkaline phosphatase nascent polypeptides on membranes of Escherichia coli.

Cancedda R, SCHLESINGER M J Bacteriol. 1974; 117(1):290-301.

PMID: 4587609 PMC: 246556. DOI: 10.1128/jb.117.1.290-301.1974.

Pleiotropic effects of mutations involved in the regulation of Escherichia coli K-12 alkaline phosphatase.

Morris H, SCHLESINGER M, Bracha M, Yagil E J Bacteriol. 1974; 119(2):583-92.

PMID: 4212247 PMC: 245645. DOI: 10.1128/jb.119.2.583-592.1974.