McLaughlin G L, Saz H J, deBruyn B S
Comp Biochem Physiol B. 1986;83(3):523-7. doi: 10.1016/0305-0491(86)90290-7.
An acyl CoA transferase has been purified to electrophoretic homogeneity from the soluble compartment of Ascaris suum muscle mitochondria. From SDS-PAGE, isoelectric focusing and molecular exclusion chromatography, homogeneity was confirmed and the enzyme appears to be composed of two similar or identical subunits of apparent mol. wts of 50,000 resulting in an apparent mol. wt of 100,000 for the holoenzyme. The apparent isoelectric point was 5.6 +/- 0.1 by both chromatofocusing columns and slab gel isoelectric focusing. The transferase was relatively specific for the short, straight-chain acyl CoA donors as well as the CoA acceptors, being active on acetyl CoA, propionyl CoA, butyryl CoA, valeryl CoA and hexanoyl CoA as donors to acetate and propionate. Neither succinyl CoA nor succinate were appreciably active as CoA donor or acceptor, respectively. This enzyme cannot serve physiologically to activate succinate for decarboxylation to propionate, but may serve to ensure a supply of propionyl CoA which appears to be required in catalytic amounts for the decarboxylation of succinate.
已从猪蛔虫肌肉线粒体的可溶性部分纯化出一种酰基辅酶A转移酶，达到电泳纯。通过SDS - PAGE、等电聚焦和分子排阻色谱法确认了其纯度，该酶似乎由两个表观分子量为50,000的相似或相同亚基组成，全酶的表观分子量为100,000。通过色谱聚焦柱和平板凝胶等电聚焦法测得的表观等电点均为5.6±0.1。该转移酶对短链直链酰基辅酶A供体以及辅酶A受体具有相对特异性，对乙酰辅酶A、丙酰辅酶A、丁酰辅酶A、戊酰辅酶A和己酰辅酶A作为供体与乙酸盐和丙酸盐反应具有活性。琥珀酰辅酶A和琥珀酸盐分别作为辅酶A供体或受体时活性均不明显。这种酶在生理上不能用于激活琥珀酸盐脱羧生成丙酸盐，但可能有助于确保提供催化量的丙酰辅酶A，这似乎是琥珀酸盐脱羧所必需的。
