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. 1971 Aug;124(1):25–30. doi: 10.1042/bj1240025

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

C N A Trotman 1,*, C Greenwood 1
PMCID: PMC1177109  PMID: 4942389

Abstract

Measurement of the ultraviolet circular dichroism of apo-(alkaline phosphatase) in urea solutions showed substantial denaturation in 3m-urea. A zinc-deficient mutant alkaline phosphatase behaved similarly. The stability of the enzyme in 6m-urea was followed as a function of its zinc content and was found to be dependent on the first two of the four zinc atoms bound by apoenzyme. Phosphatase activity was mostly dependent on a second pair of zinc atoms. Mn2+, Co2+, Cu2+ or Cd2+ also restored structural stability. Sedimentation-velocity and -equilibrium experiments revealed that dissociation of the dimer accompanied apoenzyme denaturation in urea concentrations of 1m or higher, without treatment with disulphide-reducing agent.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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