ATP-binding properties of P glycoprotein from multidrug-resistant KB cells.
作者： Marilyn M. Cornwell , Takashi Tsuruo , Michael M. Gottesman , Ira Pastan
DOI: 10.1096/FASEBJ.1.1.2886389
关键词: Multiple drug resistance 、 Monoclonal antibody 、 Cell culture 、 GTP' 、 Chemistry 、 Colchicine 、 Immunoprecipitation 、 Vinblastine 、 P-glycoprotein 、 Stereochemistry 、 Molecular biology
摘要: The photoaffinity reagent 8-azido-alpha-[32P]ATP was used to label a protein of 170 kDa in membrane vesicle preparations from highly multidrug-resistant cell line, KB-V1, but not the drug-sensitive parental line KB-3-1. 170-kDa labeled immunoprecipitated with monoclonal antibody (MRK-16) P glycoprotein. Both ATP and GTP inhibited labeling by 8-azido-alpha-[32P]ATP. Labeling P170 5 mM ADP, ribose-5-phosphate, or 100 microM vinblastine. These data directly demonstrate that glycoprotein has nucleotide-binding site could supply energy for drug transport.
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