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Ca2+-dependent and phorbol ester activating phosphorylation of a 36K-dalton protein of rat basophilic leukemia cell membranes and immunoprecipitation of the phosphorylated protein with IgE-anti IgE system |
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| Authors: | R Teshima H Ikebuchi T Terao |
| Institution: | Department of Radiochemistry, National Institute of Hygienic Sciences, 1-18-1, Kamiyoga, Setagaya-ku, Tokyo 158, Japan |
| Abstract: | Endogeneous phosphorylation of rat basophilic leukemia cell membranes was investigated. EGTA specifically inhibited the phosphorylation of a protein having an approximate molecular weight of 36,000 dalton (36K-Da protein). Phosphorylation of this protein was enhanced by phorbol-12-myristate-13-acetate in the presence of phosphatidylserine. The phosphorylated 36K-Da protein was specifically immunoprecipitated with IgE and anti IgE antibody. These results suggest that the phosphorylated 36K-Da protein is the beta-chain of the receptor for IgE and that protein kinase C is involved in the phosphorylation mechanism. |
| Keywords: | IgE immunogloblin E EGTA ethylene glycol bis(β-aminoethylether)-N N N′ N′-tetraacetic acid SDS-PAGE sodium dodecyl sulfate polyacrylamide gel electrophoresis PMA phorbol-12-myristate-13-acetate protein kinase C PS phosphatidyl serine |
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