Stam H, Hülsmann W C
Biochem Int. 1983 Aug;7(2):187-95.
The alkaline, heparin-releasable lipoprotein lipase (LPL) activity of isolated, perfused rat hearts was compared with the residual neutral lipase (NL) activity detectable in the post nuclear supernatant (PNS) from a tissue homogenate. Both enzyme activities were increased by serum, heparin and apolipoprotein CII, inhibited by high salt concentrations and by immunotitration with an anti-LPL gamma-globulin fraction. Protamine sulphate from saline liver inhibited LPL activity and the NL activity only in the absence of serum. Incubation of the PNS NL under classic conditions of hormonal stimulation (by phosphorylation) did not alter its activity and upon short-term preperfusion of the hearts with norepinephrine and glucagon also unchanged LPL and NL activities were measured. Our experiments are indicative of a possible similarity between vascular LPL and tissue NL and show that the lipase activities are not sensitive towards hormonal stimulation.
将分离的灌注大鼠心脏的碱性、可释放肝素的脂蛋白脂肪酶（LPL）活性与组织匀浆的核后上清液（PNS）中可检测到的残留中性脂肪酶（NL）活性进行了比较。血清、肝素和载脂蛋白CII均可增加这两种酶的活性，高盐浓度以及用抗LPLγ球蛋白组分进行免疫滴定可抑制它们的活性。来自生理盐水肝脏的硫酸鱼精蛋白仅在无血清时抑制LPL活性和NL活性。在经典的激素刺激条件下（通过磷酸化）孵育PNS NL不会改变其活性，并且在用去甲肾上腺素和胰高血糖素对心脏进行短期预灌注后，测得的LPL和NL活性也未改变。我们的实验表明血管LPL和组织NL之间可能存在相似性，并表明脂肪酶活性对激素刺激不敏感。
