Purification and properties of a pantetheine-hydrolyzing enzyme from pig kidney.
作者： C T Wittwer , D Burkhard , K Ririe , R Rasmussen , J Brown
DOI: 10.1016/S0021-9258(17)44559-5
关键词:
摘要: A microsomal glycoprotein that catalyzes the hydrolysis of pantetheine to pantothenate and cysteamine was solubilized purified homogeneity as determined by sodium dodecyl sulfate electrophoresis. The enzyme from pig kidney cortex on exposure butanol heat treatment, ammonium fractionation, hydrophobic chromatography, hydroxyapatite chromatography. (Mr = 57,000) has a specific activity 14 mumol produced per min/mg protein, value 35 times previously reported. method for localizing enzymatic polyacrylamide gels is presented, activity, carbohydrate are shown migrate identically electrophoresis nondenaturing gels. Amino acid analysis indicated an absorbance index E1%1cm (280 nm) 11.3, revealed presence galactose, mannose, fucose, glucose, galactosamine, sialic total composition 11.8%. various analogs had high specificity moiety but low portion.
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