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- W1034352998 abstract "Publisher Summary This chapter illustrates assay, purification, and properties of pantetheine. The enzymatic hydrolysis of pantetheine to pantothenate and cysteamine is the final common reaction in the degradation of the coenzymes phosphopantetheine and coenzyme A to the vitamin pantothenic acid. The enzymatic hydrolysis of pantetheine has been monitored by separation of radiolabeled substrate and product by electrophoresis, pH-stat titration of reaction products, and amino acid analysis of the N-ethylmaleimide adduct of cysteamine. The radiolabeled assay is best used on tissue homogenates, whereas the continuous mercaptide assay is more convenient for partially purified preparations. Radiolabeled substrate and product are separated by a fast paper chromatography system and quantified by liquid scintillation counting. Activity on nondenaturing polyacrylamide gels is visualized by local titration of cresol red. The enzymatic reaction produces acid at pH values intermediate to the pK values of pantetheine and cysteamine. The enzyme is activated by thiols and inhibited by thiol inhibitors. The enzyme is a glycoprotein containing 11.8% carbohydrate by weight. Pantetheine hydrolase activity has been identified in human fibroblasts and white blood cells and in several organs of mammalian species." @default.
- W1034352998 created "2016-06-24" @default.
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- W1034352998 date "1986-01-01" @default.
- W1034352998 modified "2023-09-25" @default.
- W1034352998 title "[7] Enzymatic hydrolysis of pantetheine" @default.
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- W1034352998 doi "https://doi.org/10.1016/0076-6879(86)22145-x" @default.
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