Characterization of purified insulin receptor subunits.
نویسندگان
چکیده
منابع مشابه
Phosphorylation of purified insulin receptor by cAMP kinase.
Highly purified insulin receptor was shown to be a substrate for cAMP kinase. Approximately 1 phosphate was incorporated per molecule of receptor, and the cAMP kinase's affinity for the receptor was at least as high as its affinity for histone. The sites phosphorylated by cAMP kinase seemed distinct from those phosphorylated by the protein kinase C. Phosphorylation by cAMP kinase had no effect ...
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We have identified the subunits of the insulin receptor using immunoprecipitation by antibodies to the insulin receptor after either biosynthetic or surface labeling of cultured human lymphocytes (I"9). With this approach, we have found there are two major, M, = 135,000 (a), M, = 95,000 @) and one minor, M, = 210,000 ( y ) subunit. Peptide mapping clearly demonstrates that the major peptides of...
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Two methods were used to label insulin receptors covalently with 125I. In the first, an aryl azide derivative of insulin, 125I-labeled 4-azido-2-nitrophenyl-insulin, was synthesized and used to photolabel the binding region of the insulin receptor in rat liver membranes and human placenta membranes. In the second, insulin receptors were purified from rat liver membranes and labeled with 125I by...
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Background γ-Aminobutyric acid (GABA) is considered to be the predominant inhibitory neurotransmitter in mammalian central nervous systems (CNS). There are two major classes of GABA receptors: GABAARs and GABABRs. The GABAA receptor is derived from various subunits such as alpha1-alpha 6, beta1-beta 3, gamma1-gamma 4, delta, epsilon, pi, and rho1-3. Intensive research has been performed to und...
متن کاملPhosphorylation--dephosphorylation of purified insulin receptor from human placenta. Effect of insulin.
The insulin receptor of human placenta even after extensive purification is phosphorylated in the presence of [gamma-32P]ATP and NaF, and is dephosphorylated again on incubation in NaF-free medium. Insulin stimulates phosphate incorporation into the Mr 95 000 subunit probably by activation of the phosphorylation step. Our data suggest that the insulin receptor contains both kinase and phosphata...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)43589-7