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Partial purification and specificity of triacylglycerol: Sterol acyltransferase from Sinapis alba
Authors:Jan Zimowski  Zdzis?aw A Wojciechowski
Institution:Department of Biochemistry, Warsaw University, 02-089 Warszawa, al. Zwirki i Wigury 93, Poland
Abstract:Triacylglycerol: sterol acyltransferase is present in roots of Sinapis alba seedlings. The enzyme is located predominantly in the cell membrane structures sedimenting at 300–16 000 g but can be solubilized by acetone treatment and buffer extraction. During gel filtration on Sephadex G-100 the acyltransferase activity was separated into two peaks corresponding to MW 1.8 × 1014 and MW ? 105, respectively. A number of natural 3β-hydroxysterols can be esterified by the solubilized acyltransferase. The rate of esterification is much higher for sterols containing a planar ring system. The number and position of double bonds, as well as the structure of the side chain at C- 17 of the sterol molecule, are of secondary importance. Triacylglycerols containing fatty acids C, C6-C22 can be utilized as acyl donors. Among triacylglycerols containing saturated fatty acids, tripalmitoylglycerol (C16:0) is the best acyl donor. For triacylglycerols containing C18-fatty acids the following sequence was observed: trioleoylglycerol (C18:1) > trilinoleoylglycerol (C18:2) > trilinolenoylglycerol (C18:3) > tristearoylglycerol (C18:0).
Keywords:steryl esters  triacylglycerol: sterol acyltransferase  enzymatic acyl transfer  
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