Bauer J E
Department of Physiological Sciences, J.H. Miller Health Sciences Center, University of Florida, Gainesville 32610.
Artery. 1988;15(5):272-91.
Rabbit heart lipoprotein lipase (LPL) was partially purified by affinity chromatography. The purified enzyme was characterized by salt inhibition, the requirement of a serum co-factor and an alkaline pH optimum. Because of the known hypocholesterolemic effect of dietary polyunsaturated fat in this and other species, the fatty acyl substrate specificity of this lipase was also studied. Both saturated and unsaturated fatty acid chain hydrolysis were investigated using synacyl and mixed acyl triglyceride emulsion substrates. It was found that trans, monounsaturated and some saturated fatty acids were more favorably hydrolyzed than polyunsaturated cis fatty acids. Positional specificity was also observed. The physiological significance of these findings may relate to a) the production of lipoprotein remnant particles relatively enriched in polyunsaturated fatty acids, especially when consumed in the diet and b) the subsequent preferential delivery of these fatty acids to the liver.
兔心脏脂蛋白脂肪酶（LPL）通过亲和层析进行了部分纯化。纯化后的酶具有盐抑制特性、需要血清辅因子且最适pH呈碱性。鉴于膳食多不饱和脂肪在该物种及其他物种中已知的降胆固醇作用，还研究了这种脂肪酶的脂肪酰基底物特异性。使用合成酰基和混合酰基甘油三酯乳液底物研究了饱和脂肪酸链和不饱和脂肪酸链的水解情况。结果发现，反式脂肪酸、单不饱和脂肪酸和一些饱和脂肪酸比多不饱和顺式脂肪酸更易于水解。还观察到了位置特异性。这些发现的生理意义可能与以下方面有关：a）产生相对富含多不饱和脂肪酸的脂蛋白残粒颗粒，尤其是在饮食中摄入时；b）随后这些脂肪酸优先输送至肝脏。
