Characterization of the insulin receptor kinase purified from human placental membranes.
@article{Kasuga1983CharacterizationOT, title={Characterization of the insulin receptor kinase purified from human placental membranes.}, author={Masato Kasuga and Yoko Fujita-Yamaguchi and D L Blithe and Morris F. White and C. Ronald Kahn}, journal={The Journal of biological chemistry}, year={1983}, volume={258 18}, pages={ 10973-80 } }
The insulin receptor purified from human placenta by sequential affinity chromatography on wheat germ agglutinin- and insulin-Sepharose to near homogeneity retained tyrosine-specific protein kinase activity. This purified insulin receptor kinase specifically catalyzed the incorporation of 32P from [gamma-32P]ATP into not only the beta-subunit of the insulin receptor but also histone H2B, a synthetic peptide which is sequentially similar to the site of tyrosine phosphorylation in pp60src (a gene… CONTINUE READING
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