作者: H Hamada , T Tsuruo
DOI: 10.1016/S0021-9258(19)57324-0
关键词:
摘要: 170-180-kDa membrane glycoprotein (P-glycoprotein) associated with multidrug resistance is involved in drug transport mechanisms across the plasma of resistant cells. From sequence analysis cDNAs P-glycoprotein gene, it postulated that active drug-efflux pump function may be attributable to protein. However, purification while preserving its enzymatic activity has not been reported. In this study, we have purified from human myelogenous leukemia K562 cell line adriamycin (K562/ADM) by means one-step immunoaffinity chromatography using a monoclonal antibody against P-glycoprotein. The procedure was simple and efficiently yielded an electrophoretically homogeneous sample. By solubilization 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, found ATPase activity. This ATP hydrolysis coupled efflux anticancer drugs multidrug-resistant