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- W2014286886 abstract "An enzyme capable of hydrolyzing myo-inositol 1-phosphate was identified and partially purified from the erythrocytes of 7-day chicks. It has an apparent molecular weight of approximately 60,000, is heat stable, and has a pH of optimal activity between 6.5 and 7.3. In most regards the kinetic properties are similar to the myo-inositol 1-phosphatases of rat testis, rat mammary gland, bovine brain, and of yeast. The enzyme has an absolute requirement for a divalent cation; Mg2+ gave the greatest activity, with an optimal concentration of 2.5 mm in the standard assay employed. Zn2+, Co2+, and Mn2+ supported activity to a lesser degree. Activity was inhibited by NaF, HgCl2, and p-hydroxymercuribenzoate. myo-Inositol tetrakis (dihydrogen phosphate) and myo-inositol 1,3,4,5,6-pentakis (dihydrogen phosphate) were not substrates for this enzyme and inhibited the hydrolysis of myo-inositol 1-phosphate. Unlike other phosphatases for myo-inositol 1-phosphate, this enzyme cleaved myo-inositol 1-phosphate (Km = 8.6 × 10−5 m) and myo-inositol 2-phosphate (Km = 2.86 × 10−4 m) at approximately the same rates. It also hydrolyzed 2′-purine and pyrimidine ribonucleotides about as well as myo-inositol 1-phosphate, but was only 20–30% as active against the 3′-ribonucleotides and had scarcely any activity against the 5′-ribonucleotides. The amount of enzyme activity in erythrocytes of embryos, chicks, and mature chickens was the same (~29 μmol/ml rbc/h). The biological function of this enzyme in avian erythrocytes is unclear at this time. Other tissues containing this phosphatase also have an enzyme which synthesizes myo-inositol 1-phosphate from glucose 6-phosphate, but we have been unable to detect the presence of such an enzyme in avian erythrocytes." @default.
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- W2014286886 date "1981-09-01" @default.
- W2014286886 modified "2023-09-26" @default.
- W2014286886 title "Studies on avian erythrocyte metabolism: Purification and properties of myo-inositol 1-phosphatase from chick erythrocytes" @default.
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- W2014286886 doi "https://doi.org/10.1016/0003-9861(81)90210-1" @default.
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