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. 1968 Mar;107(2):279–283. doi: 10.1042/bj1070279

Studies on alkaline phosphatase. Phosphorylation of calf intestinal alkaline phosphatase by 32P-labelled pyrophosphate

H N Fernley 1, Sylvia Bisaz 1
PMCID: PMC1198654  PMID: 4295986

Abstract

1. A purified preparation of alkaline phosphatase from calf-intestinal mucosa was phosphorylated by 32P-labelled PPi at a serine residue on the enzyme. Under the conditions employed, up to 0·15μm-labelled sites were obtained from 1μm-[32P]PPi. 2. The phosphorylated enzyme was labile, the rate of dephosphorylation being similar to the overall rate of substrate hydrolysis. 3. A stopped-flow technique was used to determine the number of phosphomonoesterase active sites, which agreed with the number of 32P-labelled sites. 4. It is concluded that calf-intestinal alkaline phosphatase is both a phosphomonoesterase and a pyrophosphatase.

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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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