Carlson L A, Holmquist L
Acta Med Scand. 1985;217(5):491-9. doi: 10.1111/j.0954-6820.1985.tb03252.x.
The activity of lecithin: cholesterol acyl transferase (LCAT), the enzyme which catalyses the esterification of human plasma cholesterol, has been measured by two independent methods in plasma from the two known living Swedish patients with fish eye disease. The enzyme activity was in both cases about 15% of that of normal plasma. Paradoxically, however, the percentage of plasma cholesterol which was esterified was almost normal in both patients. In addition, a normal spectrum of the fatty acids of the cholesteryl esters was present indicating a normal cholesterol esterification pathway in vivo. Incubation experiments in vitro of plasma from the two patients also yielded normal cholesterol esterification rates when measured by two different methods. These paradoxical results for cholesterol esterification are discussed on the basis of the present biochemical knowledge of fish eye disease and LCAT deficiency.
卵磷脂胆固醇酰基转移酶(LCAT)是催化人体血浆胆固醇酯化的酶,已通过两种独立方法对两名已知在世的瑞典鱼眼病患者的血浆进行了该酶活性的测定。在这两种情况下,酶活性均约为正常血浆的15%。然而,矛盾的是,两名患者血浆中酯化胆固醇的百分比几乎正常。此外,胆固醇酯脂肪酸谱正常,表明体内胆固醇酯化途径正常。通过两种不同方法对两名患者的血浆进行体外孵育实验,测得的胆固醇酯化率也正常。基于目前对鱼眼病和LCAT缺乏症的生化认识,对这些胆固醇酯化的矛盾结果进行了讨论。