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- W2101479999 abstract "A nucleoside-dependent protein kinase (EC 2.7.1.37) was partially purified from Trypanosoma gambiense, the pathogenic agent of sleeping sickness. This enzyme catalyzes the phosphorylation of histone and protamine. Various nucleosides at the concentration of 10−4 M stimulated the histone kinase activity about two-fold, whereas cyclic AMP and cyclic GMP were without effect. The pH-optimum for histone phosphorylation was at about pH 7.0. The enzyme activity absolutely depends on Mg2+, Mn2+ or Co2+. The apparent Km-value for histone was 0.3 mg/ml and those for ATP were 2 · 10−4 M and 6 · 10−5M in the absence or presence of 10−4 M adenosine, respectively. IDP and ADP compete with ATP. The inhibition constants were calculated to be 2 · 10−4 M and 2.5 · 10−4 M, respectively. The molecular weight of the histone kinase was found to be 95 000 by gel filtration and 88 000 by sedimentation in a sucrose gradient." @default.
- W2101479999 created "2016-06-24" @default.
- W2101479999 creator A5032210073 @default.
- W2101479999 date "1976-03-01" @default.
- W2101479999 modified "2023-09-27" @default.
- W2101479999 title "Nucleoside-dependent protein kinase from Trypanosoma gambiense" @default.
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- W2101479999 doi "https://doi.org/10.1016/0005-2744(76)90036-x" @default.
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