Phosphorylation—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 [γ- 32P]ATP and NaF, and is dephosphorylated again on incubation in NaF-free medium. Insulin stimulates phosphate incorporation into the M r95 000 subunit probably by activation of the phosp...
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Veröffentlicht in: | FEBS letters 1982-11, Vol.149 (1), p.96-100 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The insulin receptor of human placenta even after extensive purification is phosphorylated in the presence of [γ-
32P]ATP and NaF, and is dephosphorylated again on incubation in NaF-free medium. Insulin stimulates phosphate incorporation into the
M
r95 000 subunit probably by activation of the phosphorylation step. Our data suggest that the insulin receptor contains both kinase and phosphatase activities that may control the phosphorylation state of the receptor. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(82)81079-X |