作者: Uri Piran , Toshiro Nishida
DOI: 10.1007/BF02533465
关键词:
摘要: Highly purified lecithin-cholesterol acyltransferase of human plasma was used to study the utilization various sterols as acyl acceptor. The esterification facilitated by presence a 3β-hydroxyl group and thetrans configuration A/B rings, evident from lack acceptor activity all 3α-hydroxy tested coprostanol. Cholesterol analogs in which side chain is modified, such campesterol, β-sitosterol, desmosterol stigmasterol, were less effective than cholesterol acceptors. However, androstan-3β-o1, completely lacks chain, found be more active cholesterol. transfer required cofactor peptide apolipoprotein A-I.