酵母信号肽酶包含一种糖蛋白和Sec11基因产物。

YaDeau J T, Klein C, Blobel G

Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.

Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):517-21. doi: 10.1073/pnas.88.2.517.

Partially purified yeast microsomal signal peptidase appears to be a complex of four polypeptides of 13, 18, 20, and 25 kDa. The 18-kDa chain is the product of the Sec11 gene, which is necessary for signal peptidase activity. The 25-kDa subunit is a glycoprotein that binds Con A. Two related methods for purification of the enzyme are presented; the first includes removal of peripheral membrane proteins from microsomes by alkali extraction, solubilization of the enzyme by nonionic detergent and high salt, and four different chromatographic procedures. An alternative method was developed based on lectin-affinity chromatography.

部分纯化的酵母微粒体信号肽酶似乎是由13 kDa、18 kDa、20 kDa和25 kDa的四种多肽组成的复合物。18 kDa的链是Sec11基因的产物，该基因对于信号肽酶活性是必需的。25 kDa的亚基是一种结合伴刀豆球蛋白A的糖蛋白。本文介绍了两种相关的酶纯化方法；第一种方法包括通过碱提取从微粒体中去除外周膜蛋白，用非离子去污剂和高盐使酶溶解，以及四种不同的色谱程序。基于凝集素亲和色谱法开发了另一种方法。