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. 1965 May;95(2):475–482. doi: 10.1042/bj0950475

The metal ion activation of the alkaline β-glycerophosphatase of rabbit small intestine

B Clark 1,*, J W Porteous 1
PMCID: PMC1214346  PMID: 14340097

Abstract

1. A fraction of intestinal epithelial cells from rabbit small intestine that contained nuclei and microvillus membranes served as a source of alkaline-β-glycerophosphatase activity. 2. The greater part of the enzyme activity could be released from the subcellular particles by disintegration of the latter, followed by centrifugation at 40000g and butanol extraction of the resulting sediment. 3. Further purification of the enzyme was achieved by diethylaminoethylcellulose chromatography and by gel filtration. 4. Dialysis of the purified enzyme preparations against EDTA gave an essentially inactive enzyme. High activity could be restored by adding Zn2++Mg2+, Zn2++Co2+, Mg2++Co2+ or Co2+ alone to these inactive preparations. Neither Zn2+ nor Mg2+ added singly to the assay system restored more than a small part of the enzyme activity. 5. The optimum Zn2+ concentration was about 0·2–1m-equiv./l., whereas Mg2+ and Co2+ had optimum concentrations about 30–60m-equiv./l. 6. If added in excess of the optimum concentration, Zn2+ strongly inhibited the enzyme under all conditions tested. 7. In the presence of an optimum concentration of Co2+ (33m-equiv./l.) in tris buffer at the optimum pH (8·8 at 37°), Km for the β-glycerophosphatase was 0·3mm.

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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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