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- W1985182762 abstract "The distribution of phosphomonoesterases and phosphodiesterases in tissues of germinated barley was about 20% each for roots, shoots, and embryo, and 40% in the degermed caryopsis, expressed as a percentage of the total seedling activity. Isoelectric focusing of tissue extracts showed several phosphomonoesterases and phosphodiesterases having pI values between 4 and 6. A separate and distinct enzyme had a pI of 8·8 and was present in all tissues. This enzyme, purified by adsorption on carboxymethyl cellulose, and by gel filtration chromatography, had an apparent mol. wt. of 59,000 and catalyzed the hydrolysis of nucleoside di- and triphosphates. Treatment with sodium dodecyl sulfate and dithiothreitol apparently cleaved the enzyme into two polypeptides of equal mol. wt. The enzyme was particularly active on orthophosphate esters of p -nitrophenol. It was inactive on nucleoside monophosphates, sugar phosphates, phytate, β-glycerophosphate, pyrophosphate, pyridoxal phosphate, pyridoxamine phosphate, 5′-uridine diphosphoglucose, and dinucleoside phosphates. Activity was not stimulated by cations. Michaelis constants ranged from 0·07 to 0·37 μ M for different orthophosphate esters. The enzyme was stable at up to 60°C, and its activity was optimum at pH 7." @default.
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- W1985182762 date "1984-01-01" @default.
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- W1985182762 title "A nucleoside Di- and triphosphatase from germinating barley" @default.
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- W1985182762 doi "https://doi.org/10.1016/s0733-5210(84)80029-6" @default.
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