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- W2028832051 abstract "Incubating the soluble fraction derived from A. axanthum with phosvitin and [γ-32P]ATP results in the phosphorylation of phosvitin. Casein, histone and kemptide were practically ineffective substrates, whereas a 55 kDa protein of M. gallisepticum was efficiently phosphorylated. The enzymatic activity has an optimal pH in the pH range 6.0–6.2 and requires divalent cations. The activity was inhibited by ammonium sulfate, heparin and sulphydryl blocking reagents, but was not affected by calmodulin with or without Ca2+ or by cyclic AMP." @default.
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- W2028832051 date "1988-12-19" @default.
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- W2028832051 title "Phosvitin kinase activity in Acholeplasma axanthum" @default.
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- W2028832051 doi "https://doi.org/10.1016/0014-5793(88)80993-1" @default.
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