| Literature DB >> 40550 |
R M Dawson, N Hemington, D E Richards, R F Irvine.
Abstract
1. A phosphodiesterase that cleaves glycerophosphoinositol into glycerophosphate and inositol has been detected in rat tissues. 2. The enzyme requires Mg2+ (Mn2+) and has a pH optimum of 7.7. 3. The richest sources of the enzyme are kidney and intestinal mucosa. In pancreas subcellular fractions it occurs largely in the microsomal fraction. 4. The enzyme is inhibited by excess substrate and by the reaction product glycerophosphate. 5. Temperature-stability studies and other observations distinguish the enzyme from other membrane-bound phosphodiesterases active at an alkaline pH e.g. glycerophosphoinositol inositophosphohydrolase, glycerophosphocholine diesterase, inositol cyclic phosphate phosphodiesterase and phosphodiesterase I.Entities:
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Year: 1979 PMID: 40550 PMCID: PMC1161232 DOI: 10.1042/bj1820039
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857