期刊论文详细信息
FEBS Letters
Acylation: A new post‐translational modification specific for plasma membrane‐associated simian virus 40 large T‐antigen
Klockmann, Ulrich1  Deppert, Wolfgang1 
[1] Department of Biochemistry, University of Ulm, PO Box 4066, 7900 Ulm, FRG
关键词: Simian virus 40;    Large T-antigen;    Cell fractionation;    Post-translational modification;    Protein acylation;    Membrane-association of proteins;   
DOI  :  10.1016/0014-5793(83)80081-7
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

SV40 transformed mouse cells (mKSA) were labeled in parallel with either [35S]methionine or [3H]palmitate and subfractionated. Nuclear extracts and solubilized plasma membranes were analyzed for the presence of either 35S- or 3H-labeled SV40 large tumor antigen by immunoprecipitation and SDS polyacrylamide gel electrophoresis. The majority of the [35S]methionine labeled large T was recovered from the nuclear fraction, only minor amounts were detected in plasma membranes. In contrast, large T labeled specifically with [3H]palmitate was found only in the plasma membrane fraction. Our results demonstrate a specific acylation of large T associated with plasma membranes, suggesting that the membrane location of this predominantly nuclear protein is specific.

【 授权许可】

Unknown   

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