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
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
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
An enzyme releasing phosphocholine from glycerophosphocholine was purified to apparent homogeneity based upon SDS-PAGE. The enzyme was liberated from lyophilized bovine myelin by differential detergent extraction and final purification was accomplished with Q-Sepharose Fast Flow chromatography yielding an apparently homogeneous
In microvessels isolated from bovine brain, microsomal enzyme activities involved in phosphatidylcholine biosynthesis and degradation were determined. The microvessels possessed acyl-CoA:1-acyl-sn-glycero-3-phosphocholine (AT) and glycerophosphocholine phosphodiesterase (GroPChoPDE) activity at a higher level compared with bovine and rat brain or rat liver
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