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Molecular and cellular biochemistry, 139(2), 101-108 (1994-10-26)
The rat uterine secretory enzyme glycerylphosphorylcholine (GPC) diesterase (EC 3.1.4.2) had been purified and characterized previously with respect to its mol. wt., size, amino acid, carbohydrate composition and estrogen inducible properties. This enzyme is observed to have exclusive specificity for
Biochemistry and molecular biology international, 47(2), 283-292 (1999-04-17)
The purification and characterization of a novel phosphodiesterase (PDE) is presented. The activity was detected in the extracellular medium of Tetrahymena thermophila cultures, by the release of p-nitrophenol from p-nitrophenylphosphocholine (PNPPC) with an acidic pH optimum. In cell homogenates, it
Brain levels of glycerophosphodiesters, including glycerophosphocholine (GPC) and glycerophosphoethanolamine (GPE), are altered in many human central nervous system disorders. Although much information is available on the enzymes responsible for the formation of these phospholipid metabolites, little information is known regarding
Altered phosphatidylcholine (PC) metabolism in epithelial ovarian cancer (EOC) could provide choline-based imaging approaches as powerful tools to improve diagnosis and identify new therapeutic targets. The increase in the major choline-containing metabolite phosphocholine (PCho) in EOC compared with normal and
The Journal of biological chemistry, 283(25), 17107-17115 (2008-04-25)
The product of the open reading frame YPL206c, Pgc1p, of the yeast Saccharomyces cerevisiae displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases. Deletion of PGC1 causes an accumulation of the anionic phospholipid, phosphatidylglycerol (PG), especially under conditions of inositol limitation.
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