Abstract
Fat cells were incubated with 32P i for 2 h before the [ 32P]I-2 was immunoprecipitated, subjected to SDS PAGE , and detected by autoradiography. [ 32P]I-2 (Mr = 32,000) was not recovered when excess purified I-2 was added with the antiserum or when nonimmune serum was used. Immunoprecipitated I-2 was heat-stable, inhibited phosphatase activity, and could be synergistically phosphorylated by casein kinase II and F A GSK-3 . Several times more [ 32P]phosphoserine than [ 32P]phosphothreonine was found in I-2 from 32P-labeled cells. Insulin increased the 32P-content of I-2 by as much as 40%, suggesting that phosphorylation of I-2 might be involved in the effect of insulin on stimulating protein dephosphorylation.
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