Activity and some properties of a soluble enzyme hydrolyzing nucleoside-5'-triphosphates were studied in the liver and kidney of normal and diabetic rats. The enzyme activity was shown to be reduced by 34% (p<0.01) in the liver extracts of diabetic animals, while no difference was observed in the kidney. When ITP was used as substrate, the apparent Michaelis constant of the enzyme was significantly lower in the liver of controls as compared to experimental rats (32.3±1.3 μM and 54.3±1.0 μМ, respectively, p<0.01). The KM values of the enzyme in the kidney were not distinguishable in both groups. NTPase exhibits maximal activity at pH 7.0 and has a broad substrate specificity with respect to different nucleoside-5'-tri- and diphosphates. Molecular mass of the enzyme was estimated by gel filtration to be 63.7±0.9 kD.
Rusina I.M., Makarchikov A.F., Makar E.A., Kubyshin V.L. (2006) Nucleoside-5'-triphosphate hydrolysis in the liver and kidney of rats with chronic alloxan diabetes. Biomeditsinskaya Khimiya, 52(4), 364-369.
Rusina I.M. et al. Nucleoside-5'-triphosphate hydrolysis in the liver and kidney of rats with chronic alloxan diabetes // Biomeditsinskaya Khimiya. - 2006. - V. 52. -N 4. - P. 364-369.
Rusina I.M. et al., "Nucleoside-5'-triphosphate hydrolysis in the liver and kidney of rats with chronic alloxan diabetes." Biomeditsinskaya Khimiya 52.4 (2006): 364-369.
Rusina, I. M., Makarchikov, A. F., Makar, E. A., Kubyshin, V. L. (2006). Nucleoside-5'-triphosphate hydrolysis in the liver and kidney of rats with chronic alloxan diabetes. Biomeditsinskaya Khimiya, 52(4), 364-369.
References
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