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An affinity purified human insulin receptor preparation was shown to phosphorylate the α- and β-subunits of the guanine nucleotide-regulatory proteins G i and G o , derived from bovine brain. The presence of insulin stimulated the rate of their phosphorylation some 2-fold. The presence of G i and G o did not affect the degree of autophosphorylation of the β-subunit...
Autophosphorylation of the purified human insulin receptor tyrosyl kinase was found to be inhibited by the ras oncogene product p21 in a concentration- and GDP-dependent manner. GDP-β-S but not Gpp(NH)p could substitute for GDP in eliciting the ras-dependent inhibition. The inhibition was seen with both normal or mutant (Lys-61) p21 N-ras and normal or mutant (Val-12) p21...
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