Phosphorylation of a 16-kDa protein by diacylglycerol-activated protein kinase C in vitro and by vasopressin in intact hepatocytes |
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Authors: | R H Cooper K Kobayashi J R Williamson |
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Institution: | Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA |
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Abstract: | A replication-defective Simian virus 40 genome, with a deletion of about 120 nucleotides in the region encoding the N-terminal fourth of the large T antigen, has been isolated from the DNA of Simian cells transformed by SV40. Both the original transformants, and the murine transformants obtained by transfection with this cloned mutant DNA, produced a large T antigen displaying in immunofluorescence an exclusively cytoplasmic localization. The protein apparent molecular mass (83 kDa) was about 6% smaller than that of normal karyophilic large T. Restriction analysis showed that the deletion eliminated two close HinfI sites, at nucleotides 4459 and 4376 (map unit 0.50). |
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Keywords: | Protein phosphorylation Diacylglycerol-activated protein kinase C Vasopressin Hepatocyte Hormone action SDS sodium dodecyl sulfate |
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