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Phosphorylation—dephosphorylation of purified insulin receptor from human placenta
Author(s) -
Machicao F.,
Urumow T.,
Wieland O.H.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81079-x
Subject(s) - dephosphorylation , phosphorylation , insulin receptor , insulin receptor substrate , phosphatase , insulin , chemistry , receptor , protein subunit , irs2 , biochemistry , endocrinology , biology , insulin resistance , gene
The insulin receptor of human placenta even after extensive purification is phosphorylated in the presence of [γ‐ 32 P]ATP and NaF, and is dephosphorylated again on incubation in NaF‐free medium. Insulin stimulates phosphate incorporation into the M r 95 000 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.