Matrix-assisted laser desorption ionization mass spectrometry of membrane proteins: Demonstration of a simple method to determine subunit molecular weights of hydrophobic subunits

被引：24

作者：

Ghaim, JB ^{[1
]}

Tsatsos, PH ^{[1
]}

Katsonouri, A ^{[1
]}

Mitchell, DM ^{[1
]}

SalcedoHernandez, R ^{[1
]}

Gennis, RB ^{[1
]}

机构：

[1] UNIV ILLINOIS,DEPT BIOCHEM,URBANA,IL 61801

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 1997年 / 1330卷 / 02期

关键词：

MALDI; hydrophobic; protein; molecular mass;

D O I：

10.1016/S0005-2736(97)00127-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Matrix-assisted laser desorption ionization (MALDI) mass spectrometry has been used to obtain accurate molecular weight information for each subunit of several hydrophobic integral membrane proteins: cytochrome bo(3) (4 subunits) and cytochrome bd (2 subunits) from E. coli, and the bc(1) complex (3 subunits) and the cytochrome c oxidase (3 subunits) from Rhodobacter sphaeroides. The results demonstrate that the MALDI method is a convenient, quick, sensitive and reliable means for obtaining the molecular masses of the subunits of purified multisubunit membrane proteins. (C) 1997 Elsevier Science B.V.

引用

页码：113 / 120

页数：8

共 27 条

[1] LARGE-SCALE PURIFICATION AND CHARACTERIZATION OF A HIGHLY-ACTIVE 4-SUBUNIT CYTOCHROME BC1 COMPLEX FROM RHODOBACTER-SPHAEROIDES [J].