通过疏水色谱法从大鼠肠黏膜中纯化具有溶血磷脂酶活性的酶。
Purification of an enzyme with lysophospholipase activity from rat intestinal mucosa by hydrophobic chromatography.
作者信息
Allenmark S, Sjödahl E, Sjödahl R, Tagesson C
出版信息
Prep Biochem. 1980;10(4):463-71. doi: 10.1080/00327488008061743.
PMID:7413608
Abstract
A method based on hydrophobic chromatography is described for the purification of a lysophospholipase from the mucosa of rat small intestine. Under the conditions used, one single chromatographic run on phenyl-Sepharose CL-4B yielded a 582-fold purification with a 79% overall recovery of enzyme activity. A subsodium dodecyl sulphate gel electrophoresis; its isoelectric point is 5.6.
摘要
描述了一种基于疏水色谱法从大鼠小肠黏膜中纯化溶血磷脂酶的方法。在所使用的条件下，在苯基 - 琼脂糖CL - 4B上进行一次色谱运行，酶活性的总回收率为79%，纯化倍数达582倍。十二烷基硫酸钠凝胶电泳显示，其等电点为5.6。
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