作者: TL Swenson , JS Simmons , CB Hesler , C Bisgaier , AR Tall
DOI: 10.1016/S0021-9258(18)49249-6
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摘要: A cholesteryl ester transfer protein (CETP) of apparent Mr 74,000 has recently been purified from human plasma. Cholesteryl activity was found to accumulate in the medium cultured Hep G2 cells. The removed by immunoprecipitation with specific antibodies plasma CETP. Sodium dodecyl sulfate gel electrophoresis immunoprecipitates prepared cells pulsed [35S]methionine revealed a broad band 72,000 76,000; contrast, cellular homogenates showed sharp 58,000. 76,000 disappears, concomitant appearance lower products, upon neuraminidase or glycopeptidase F treatment results indicate that liver have capacity synthesize and secrete CETP peptide acquires asparagine-linked carbohydrate sialic acid during intracellular processing.