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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Desaturation of Myristoyi-CoA to Myristoleoyl-CoA by Hen Liver Microsomal DELTA~9-Desaturase
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Desaturation of Myristoyi-CoA to Myristoleoyl-CoA by Hen Liver Microsomal DELTA~9-Desaturase

机译:鸡肝微粒体DEL〜9-去饱和酶将Myristoyi-CoA脱饱和为Myristoleoyl-CoA

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The desaturation of myristoyl-CoA to myristoleoyl-CoA was measured in microsomal preparations of hen liver.The desaturation was maximal at pH 7.4.The enzymatic activity was linear with time up to 10 min and proportional to microsomal protein concentrations.The initial velocity was linear with substrate concentrations between 13 and up to 200muM.A decrease in desaturation activity was observed at substrate concentrations greater than 266muM.There was an absolute requirement for reduced pyridine nucleotide (NADH),while a maximum activity was observed at a myristoyl-CoA:NADH mole ratio of 1.Competitive inhibition studies of myristoyl-CoA desaturation suggest that the inhibitors,stearyl and oleyl-CoA,were more effective than palmitoyl-CoA.Free CoA did not inhibit the DELTA~9-desaturase system.The desaturation of myristoyl-CoA was stimulated by bovine serum albumin and reduced by cytoplasmic proteins.The effect of cytoplasmic proteins on the enzymatic reaction was completely abolished by trypsin digestion and boiling for 30 min.On the basis of these data,it was concluded that 9,10-desaturation of acyl-CoA derivatives containing 14-18 carbon fatty acyl chains is catalyzed by the same enzyme.
机译:在鸡肝微粒体制剂中检测到肉豆蔻酰辅酶A对肉豆蔻酰辅酶A的去饱和度,在pH 7.4时去饱和度最大,在10分钟以下的时间内酶活性呈线性,且与微粒体蛋白浓度成正比,初始速度呈线性底物浓度在13到200μM之间。当底物浓度大于266μM时观察到去饱和活性降低。绝对需要还原吡啶核苷酸(NADH),而在肉豆蔻酰-CoA:NADH时观察到最大活性1.对肉豆蔻酰辅酶A脱饱和的竞争性抑制研究表明,硬脂酸和油酰辅酶A的抑制剂比棕榈酰辅酶A更有效。游离的CoA不能抑制DELTA〜9-去饱和酶系统。牛血清白蛋白刺激辅酶A,胞质蛋白降低辅酶A。tr完全消除了胞质蛋白对酶促反应的作用。酶解并煮沸30分钟。根据这些数据,得出的结论是,相同的酶催化含有14-18个碳脂肪酰基链的酰基-CoA衍生物进行9,10-去饱和。

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