YEAST SIGNAL PEPTIDASE CONTAINS A GLYCOPROTEIN AND THE SEC11 GENE-PRODUCT

被引：53

作者：

YADEAU, JT ^{[1
]}

KLEIN, C ^{[1
]}

BLOBEL, G ^{[1
]}

机构：

[1] ROCKEFELLER UNIV,HOWARD HUGHES MED INST,CELL BIOL LAB,NEW YORK,NY 10021

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 02期

关键词：

PROTEIN PURIFICATION; YEAST MICROSOMAL MEMBRANES; INTEGRAL MEMBRANE PROTEINS; POSTTRANSLATIONAL PRECURSOR PROCESSING;

D O I：

10.1073/pnas.88.2.517

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：517 / 521

页数：5

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