Nieuwenhuizen W, Reman F C, Vermeer I A, Vermond T
Biochim Biophys Acta. 1976 May 27;431(2):288-96. doi: 10.1016/0005-2760(76)90149-1.
Two lipases were purified from pig adipose tissue after delipidation by a mild and effective procedure using mixtures of chloroform and butanol. This was followed by hydrophobic adsorption chromatography on aminohexyl-Sepharose 4B coupled with octanoic acid, gel filtration on Sephadex G-100, and isoelectric focusing. Two electrophoretically and chromatographically pure enzymes were obtained, which had the same molecular weight (60 000 +/- 3000) and specific activity, and almost identical amino acid compositions; the isoelectric points, i.e. 5.2 and 5.5, differed.
采用温和有效的方法，用氯仿和丁醇混合物对猪脂肪组织进行脱脂后，从中纯化出了两种脂肪酶。接着进行了以下操作：在偶联辛酸的氨基己基-琼脂糖4B上进行疏水吸附色谱，在葡聚糖G-100上进行凝胶过滤，以及进行等电聚焦。得到了两种电泳和色谱纯的酶，它们具有相同的分子量（60000±3000）和比活性，氨基酸组成几乎相同；等电点不同，分别为5.2和5.5。
