大鼠肝脏微粒体中硬脂酸去饱和作用：脂肪酸结合蛋白的刺激作用

Stearic acid desaturation in rat liver microsomes: stimulation by fatty acid binding protein.

作者信息

Catalá A

出版信息

Acta Physiol Pharmacol Latinoam. 1986;36(1):19-27.

Abstract

A soluble protein (Mr = 12,000) showing the characteristics of fatty acid binding protein is partially purified from rat liver cytosol (15-fold on the basis of its affinity for oleic acid) using ammonium sulphate precipitation. More oleate than stearate is removed from liver microsomes incubated with similar amounts of both fatty acids and the protein, indicating that it has a higher affinity for oleic than for stearic acid. When added to microsomes, a fraction enriched in this protein stimulates stearic acid desaturation. Such an effect is abolished if the protein is pre-saturated with oleic acid. It is suggested that the stimulation of stearic acid desaturation by fatty acid binding protein may involve a selective removal of the product, oleic acid, from the microsomal membranes.

摘要

一种具有脂肪酸结合蛋白特征的可溶性蛋白（分子量为12,000），通过硫酸铵沉淀法从大鼠肝细胞溶质中部分纯化（基于其对油酸的亲和力提高了15倍）。在与等量的油酸和硬脂酸以及该蛋白一起孵育的肝微粒体中，从肝微粒体中去除的油酸比硬脂酸多，这表明它对油酸的亲和力高于硬脂酸。当添加到微粒体中时，富含这种蛋白的部分会刺激硬脂酸去饱和作用。如果该蛋白预先用油酸饱和，则这种作用会被消除。有人提出，脂肪酸结合蛋白对硬脂酸去饱和作用的刺激可能涉及从微粒体膜中选择性去除产物油酸。