Ashby P, Tolson A M, Robinson D S
Biochem J. 1978 May 1;171(2):305-11. doi: 10.1042/bj1710305.
Lipoprotein lipase is heterogeneous, and it was suggested that the enzyme in adipose tissue is transformed from a species of mol. wt. approx. 120000 to forms of much higher molecular weight as it is secreted from the fat-cell. This paper demonstrates that the forms of higher molecular weight are probably artifacts. Enzyme preparations were characterized by gel filtration, by density-gradient centrifugation and by affinity chromatography. The results indicate that the enzyme forms of mol. wt. greater than 120000 result from an association of the enzyme with particulate material. It is therefore necessary to reconsider schemes that have recently been proposed for the synthesis and export of lipoprotein lipase.
脂蛋白脂肪酶具有异质性，有人提出脂肪组织中的这种酶是由一种分子量约为120000的分子转变而来的，随着它从脂肪细胞分泌出来，会形成分子量高得多的形式。本文证明，分子量较高的形式可能是人为产物。通过凝胶过滤、密度梯度离心和亲和色谱对酶制剂进行了表征。结果表明，分子量大于120000的酶形式是酶与颗粒物质结合的结果。因此，有必要重新考虑最近提出的脂蛋白脂肪酶合成和分泌的方案。
