从发育的红花种子的微粒体中酰基辅酶 A：O-溶血磷脂酰基转移酶的增溶和特性描述。
Solubilization and Characterization of an Acyl-Coenzyme A : O-LYSOPHOSPHOLIPID ACYLTRANSFERASE FROM THE MICROSOMES OF DEVELOPING SAFFLOWER SEEDS.
机构信息
Department of Biochemistry and Biophysics, University of California, Davis, California 95616.
出版信息
Plant Physiol. 1982 Jun;69(6):1293-7. doi: 10.1104/pp.69.6.1293.
Abstract
Acyl-CoA:O-lysophospholipid acyltransferase activity was measured in extracts of developing safflower (Carthamus tinctorius var. UC-1) seeds. Acyltransferase activity was present in all subcellular fractions. The microsomal acyltransferase activity was solubilized with either 30 mm-n-octylglucoside, 1% deoxycholate, or 100 mum lysophosphatidylcholine. The pH optimum of the lysophosphatidylcholine-dependent acyltransferase activity was at 9.0. Among the various acyl-CoA's tested, oleoyl-CoA was the best substrate and with it the enzyme had a K(m) of 9.5 mum. Among the various acyl acceptors tested, lysophosphatidylcholine (oleoyl) gave the highest activity and the optimal concentration was 30 mum. Acyltransferase activity was stimulated by ethanol and inhibited by bovine serum albumin and divalent cations.
摘要
酰基辅酶 A：溶血磷脂酰基转移酶活性在发育中的红花（Carthamus tinctorius var. UC-1）种子的提取物中进行了测量。酰基转移酶活性存在于所有亚细胞部分中。用 30mm-n-辛基葡糖苷、1%脱氧胆酸钠或 100µM 溶血磷脂酰胆碱可溶解微粒体酰基转移酶活性。溶血磷脂酰胆碱依赖性酰基转移酶活性的 pH 最适值为 9.0。在所测试的各种酰基辅酶 A 中，油酰基辅酶 A 是最佳底物，酶的 K(m)为 9.5µM。在所测试的各种酰基受体中，溶血磷脂酰胆碱（油酰基）给出了最高的活性，最佳浓度为 30µM。酰基转移酶活性受到乙醇的刺激，受到牛血清白蛋白和二价阳离子的抑制。
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