SCANU A, ORIENTE P
J Exp Med. 1961 Apr 1;113(4):735-57. doi: 10.1084/jem.113.4.735.
Triton WR-1339, a non-ionic detergent, added to canine serum or to ultracentrifugally separated lipoproteins, induced changes in the lipoproteins which were dependent upon concentration of detergent and class of lipoproteins. D 1.063 to 1.21 lipoprotein (alpha-LP) was especially sensitive to the action of triton. Addition of 2 mg. of triton to 1 mg. of alpha-LP (based on protein content), induced only slight changes in the electrophoretic and flotation characteristics of the lipoprotein. With a tenfold increase of the detergent (triton:alpha-LP, 20:1), the mixture, analyzed by starch gel and paper electrophoresis, yielded a tritonlipid complex which remained close to the origin, and a nearly lipid-free protein with electrophoretic mobility higher (starch gel) or lower (paper) than native alpha-LP. The splitting of the lipid and protein moieties of alpha-LP could not be clearly shown when the same mixture was analyzed by free boundary electrophoresis. Triton alone moved only slightly in an electrical field (paper, starch gel, Tiselius); it sedimented during ultracentrifugation at D 1.006 and D 1.063 and floated at D 1.21. D 1.006 to 1.063 lipoproteins (beta-LP), required larger amounts of triton to show changes. These were evident in 40 to 80:1 mixtures of triton and beta-LP. In starch gel and paper electrophoresis triton retained, in a position close to the origin, part of the lipids of beta-LP; the remaining beta-LP fraction, impoverished of lipids, had electrophoretic mobility similar to native beta-LP. The triton-lipid complex sedimented at D 1.063. After addition of triton to complexes [chylomicron-alpha-P-I(131)] or [lipomul-alpha-LP-1(131)], the electrophoretic and ultracentrifugal analyses of these mixtures revealed that the labeled protein was removed from the triglyceride component. Triton also prevented the occurrence of the interaction between lipomul and alpha-LP and the hydrolysis of both chylomicrons and lipomul-alpha-LP by lipoprotein lipase. It is postulated that, if the changes in lipoproteins and chylomicrons observed in vitro occur in vivo, they could account, at least in part, for the hyperlipemia which develops in animals following administration of triton.
非离子去污剂曲通WR - 1339添加到犬血清或超速离心分离的脂蛋白中,会引起脂蛋白的变化,这些变化取决于去污剂的浓度和脂蛋白的类别。密度为1.063至1.21的脂蛋白(α - LP)对曲通的作用特别敏感。向1毫克α - LP(基于蛋白质含量)中添加2毫克曲通,仅引起脂蛋白电泳和漂浮特性的轻微变化。当去污剂增加十倍(曲通:α - LP,20:1)时,通过淀粉凝胶和纸电泳分析该混合物,会产生一种靠近原点的曲通 - 脂质复合物,以及一种几乎无脂质的蛋白质,其电泳迁移率比天然α - LP高(淀粉凝胶)或低(纸电泳)。当用自由界面电泳分析相同混合物时,α - LP的脂质和蛋白质部分的分离并不明显。单独的曲通在电场(纸电泳、淀粉凝胶电泳、Tiselius电泳)中移动很少;它在密度为1.006和1.063时超速离心时沉降,在密度为1.21时漂浮。密度为1.006至1.063的脂蛋白(β - LP)需要大量曲通才会出现变化。在曲通与β - LP比例为40至80:1的混合物中这些变化很明显。在淀粉凝胶和纸电泳中,曲通在靠近原点的位置保留了β - LP的部分脂质;剩余的贫脂β - LP部分,其电泳迁移率与天然β - LP相似。曲通 - 脂质复合物在密度为1.063时沉降。向复合物[乳糜微粒 - α - P - I(131)]或[脂质乳剂 - α - LP - 1(131)]中添加曲通后,对这些混合物的电泳和超速离心分析表明,标记的蛋白质从甘油三酯成分中被去除。曲通还阻止了脂质乳剂与α - LP之间的相互作用以及脂蛋白脂肪酶对乳糜微粒和脂质乳剂 - α - LP的水解。据推测,如果在体外观察到的脂蛋白和乳糜微粒的变化在体内发生,它们至少可以部分解释动物在给予曲通后出现的高脂血症。