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- W2087150905 abstract "Examination of prostasomes, isolated from human seminal plasma, showed that there was very little remaining paranitrophenylphosphatase activity when assayed in the presence of 10 mmol/l of tartrate and 2 mmol/l of levamisole. Under these conditions it was possible to study the prostasome membrane-bound 5′-nucleotidase activity, which was unaffected by these two inhibitors. The activity was considered to be located at the external surface of the prostasome membrane and a 50–60% increase in activity was obtained by the addition of 0.05% Triton X-100. The prostasome membrane-linked 5′-nucleotidase readily hydrolysed 5′-AMP. Two other 5′-nucleoside monophosphates, 5′-IMP and 5′-GMP, were also hydrolysed, but more slowly; 2′- or 3′-AMP were practically not attacked. The prostasome membrane-linked 5′-nucleotidase obeyed Michaelis-Menten kinetics. Apparent Km for 5′-AMP was 11.2 ± 2.1 μmol/l and Vmax 64.7 ± 11.4 nmol/mg protein/min. These figures were somewhat changed in presence of 0.05% Triton X-100, the Km value being reduced by 30% and the Vmax value increased by 60%. Adenosine 5′ (α, β methylene) diphosphate (100 μmol/l), Ni2+ (10 mmol/l) and concanavalin A (20 μg/ml) were all potent inhibitors of the prostasome membrane-linked 5′-nucleotidase." @default.
- W2087150905 created "2016-06-24" @default.
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- W2087150905 date "1993-07-01" @default.
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- W2087150905 title "Characteristics of membrane-bound 5′-nucleotidase on human prostasomes" @default.
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- W2087150905 doi "https://doi.org/10.1016/0009-8981(93)90150-3" @default.
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