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Correlation of acidic and basic carrier ampholyte and immobilized pH gradient two‐dimensional gel electrophoresis patterns based on mass spectrometric protein identification

Correlation of acidic and basic carrier ampholyte and immobilized pH gradient two‐dimensional gel... Separation of proteins on either carrier ampholyte‐based or immobilized pH gradient‐based two‐dimensional (2‐D) gels gives rise to electrophoretic patterns that are difficult to compare visually. In this paper we have used matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) to determine the identities of 335 protein spots in these two 2‐D gel systems, including a substantial number of basic proteins which had never been identified before. Proteins that were identified in both gel systems allowed us to cross‐reference the gel patterns. Vector analysis of these cross‐references demonstrated that there is no obvious pattern by which the mobility of a protein in one gel system can be used to predict its mobility in the other. Thus, as laboratories adopt the immobilized pH gradient‐based 2‐D gel systems, the only reliable means of translating the data gained with the carrier ampholyte‐based gel system is to positively identify the proteins in both 2‐D systems. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Electrophoresis Wiley

Correlation of acidic and basic carrier ampholyte and immobilized pH gradient two‐dimensional gel electrophoresis patterns based on mass spectrometric protein identification

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References (33)

Publisher
Wiley
Copyright
"Copyright © 1998 Wiley Subscription Services, Inc., A Wiley Company"
ISSN
0173-0835
eISSN
1522-2683
DOI
10.1002/elps.1150190618
pmid
9638949
Publisher site
See Article on Publisher Site

Abstract

Separation of proteins on either carrier ampholyte‐based or immobilized pH gradient‐based two‐dimensional (2‐D) gels gives rise to electrophoretic patterns that are difficult to compare visually. In this paper we have used matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) to determine the identities of 335 protein spots in these two 2‐D gel systems, including a substantial number of basic proteins which had never been identified before. Proteins that were identified in both gel systems allowed us to cross‐reference the gel patterns. Vector analysis of these cross‐references demonstrated that there is no obvious pattern by which the mobility of a protein in one gel system can be used to predict its mobility in the other. Thus, as laboratories adopt the immobilized pH gradient‐based 2‐D gel systems, the only reliable means of translating the data gained with the carrier ampholyte‐based gel system is to positively identify the proteins in both 2‐D systems.

Journal

ElectrophoresisWiley

Published: May 1, 1998

Keywords: ;

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