| Literature DB >> 4295986 |
Abstract
1. A purified preparation of alkaline phosphatase from calf-intestinal mucosa was phosphorylated by (32)P-labelled PP(i) at a serine residue on the enzyme. Under the conditions employed, up to 0.15mum-labelled sites were obtained from 1mum-[(32)P]PP(i). 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 (32)P-labelled sites. 4. It is concluded that calf-intestinal alkaline phosphatase is both a phosphomonoesterase and a pyrophosphatase.Entities:
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Year: 1968 PMID： 4295986 PMCID： PMC1198654 DOI： 10.1042/bj1070279
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857