Van Dessel G, Lagrou A
UIA-Laboratory for Pathological Biochemistry, Belgium.
Acta Biochim Pol. 1994;41(3):311-20.
A protein catalyzing dolichol transfer between membranes has been purified from bovine liver up to 600-fold by acid precipitation, ammonium sulfate precipitation, ion-exchange chromatography and hydrophobic interaction chromatography. The protein displays a relative molecular mass of 15000 on SDS-gel electrophoresis. Kinetics as well as the influence of a series of effectors were studied. The transfer activity is inhibited by sphingomyelin, sulfhydryl groups and cationic amphiphilic amines with a bulky heterocyclic aromatic function. High salt concentration decreases the transfer efficiency. Transfer of dolichol between vesicles and mitochondria is not affected by the presence of moderate amounts of cholesterol in the donor vesicles. The overall characteristics of dolichol transfer activity are discussed in comparison to these of other lipid transfer proteins.
一种催化膜间多萜醇转移的蛋白质已通过酸沉淀、硫酸铵沉淀、离子交换色谱和疏水相互作用色谱从牛肝中纯化出来，纯化倍数高达600倍。该蛋白质在SDS凝胶电泳上显示的相对分子质量为15000。研究了其动力学以及一系列效应物的影响。鞘磷脂、巯基和具有庞大杂环芳香功能的阳离子两亲胺可抑制转移活性。高盐浓度会降低转移效率。供体囊泡中存在适量胆固醇不会影响多萜醇在囊泡和线粒体之间的转移。与其他脂质转移蛋白相比，讨论了多萜醇转移活性的总体特征。
