Increasing: Charge While Preserving Noncovalent Protein Complexes for ESI-MS

被引：131

作者：

Lomeli, Shirley H.

Yin, Sheng

Loo, Rachel R. Ogorzalek ^{[2
]}

Loo, Joseph A. ^{[1
,2
]}

机构：

[1] Univ Calif Los Angeles, Inst Mol Biol, Dept Chem & Biochem, Los Angeles, CA 90095 USA

[2] Univ Calif Los Angeles, David Geffen Sch Med, Dept Biol Chem, Los Angeles, CA 90095 USA

来源：

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY | 2009年 / 20卷 / 04期

基金：

美国国家卫生研究院;

关键词：

IONIZATION MASS-SPECTROMETRY; ELECTROSPRAY-IONIZATION; ACTIVATED DISSOCIATION; STATE DISTRIBUTIONS; SURFACE-TENSION; SOLVENT; PEPTIDE; POLYPEPTIDES;

D O I：

10.1016/j.jasms.2008.11.013

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Increased multiple charging of native proteins and noncovalent protein complexes is observed in electrospray ionization (EST) mass spectra obtained from nondenaturing protein solutions containing up to 1% (vol/vol) m-nitrobenzyl alcohol (m-NBA). The increases in charge ranged from 8% for the 690 kDa alpha(7)beta(7)beta(7)alpha(7) 20S proteasome complex to 48% additional charge for the zinc-bound 29 kDa carbonic anhydrase-II protein. No dissociation of the noncovalently bound ligands/subunits was observed upon the addition of m-NBA. It is not clear if the enhanced charging is related to altered surface tension as proposed in the "supercharging" model of Iavarone and Williams (Iavarone, A. T.; Williams, E. R. J. Am. Chem. Soc. 2003, 125, 2319-2327). However, more highly charged noncovalent protein complexes have utility in relaxing slightly the mass-to-charge (m/z) requirements of the mass spectrometer for detection and will be effective for enhancing the efficiency for tandem mass spectrometry studies of protein complexes. (J Am Soc Mass Spectrom 2009, 20, 593-596) (C) 2009 Published by Elsevier Inc. on behalf of American Society for Mass Spectrometry

引用

页码：593 / 596

页数：4

共 27 条

[1] Gas-phase proton-transfer chemistry coupled with TOF mass spectrometry and ion mobility-MS for the facile analysis of poly(ethylene glycols) and PEGylated polypeptide conjugates [J].