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McArdle Laboratory for Cancer Research, University of Wisconsin, Madison, Wisconsin 53706
Protein kinase activity copurified with the receptor for 12-O-[3H]tetradecanoylphorbol-13-acetate during its purification from mouse brain particulate protein. All attempts to resolve the protein kinase activity from the receptor were unsuccessful. The isolated receptor required phospholipid and divalent calcium for maximal portein kinase activity. The protein kinase was not activated by cyclic nucleotides or calmodulin. There are striking similarities between the receptor-associated protein kinase activity and the calcium- and phospholipid-dependent protein kinase, which has been suspected of mediating the effects of biological stimuli associated with increased phosphatidylinositol turnover.
1 Supported by NIH Grants CA-09135, CA-22484, and CA-07175. This is Paper 2 of 2 articles on the biochemical nature of the phorbol ester receptor. Paper 1 (2) describes the isolation of this receptor from mouse brain particulate protein.
2 Present address: Department of Medicinal Chemistry, Pharmacy Building, Purdue University, W. Lafayette, Ind. 47907. To whom requests for reprints should be addressed.
Received 10/28/82. Accepted 6/ 8/83.
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