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- W1983129580 abstract "Cationic cofactors (e.g., polylysine or histone H2B) are necessary to observe phosphorylation of calmodulin in cell-free systems containing partially purified insulin receptors from a variety of tissues. The highly basic carboxyl terminus of the human c-Ki-ras 2 gene product stimulated both the invitro phosphorylation of calmodulin and autophosphorylation of the β-subunit of the insulin receptor, independently of insulin. Addition of insulin increased phosphate incorporation into calmodulin 2.5 fold. The K0.5 for insulin was approximately 5 × 10−8 M. Maximal phosphorylation occurred at 120μM c-Ki- ras 2 in the absence of Ca2+ and was inhibited by free Ca2+ concentrations above 0.1μM. These data suggest the c-Ki-ras 2 gene product, an endogenous membrane protein, may play an important role in the cellular mechanism of insulin action." @default.
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- W1983129580 date "1989-06-01" @default.
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- W1983129580 title "The carboxyl terminal segment of the c-Ki-rask 2 gene product mediates insulin-stimulated phosphorylation of calmodulin and stimulates insulin-independent autophosphorylation of the insulin receptor" @default.
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- W1983129580 doi "https://doi.org/10.1016/0006-291x(89)92612-0" @default.
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