Premium
Protein tryptic digests analyzed by carrier ampholyte‐based capillary electrophoresis coupled to ESI‐MS
Author(s) -
Busnel JeanMarc,
Descroix Stéphanie,
Le Saux Thomas,
Terabe Shigeru,
Hennion MarieClaire,
Peltre Gabriel
Publication year - 2006
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200500808
Subject(s) - chemistry , chromatography , capillary electrophoresis , cytochrome c , joule heating , electrophoresis , capillary action , analytical chemistry (journal) , biochemistry , mitochondrion , materials science , composite material , electrical engineering , engineering
In this study, narrow pH cuts of carrier ampholytes have been used as buffers in CE for the analysis of protein tryptic digests. Their low conductivity allows very efficient separations under high electric field strength without inducing any significant Joule heating. In this study, the capabilities of narrow pH cuts of carrier ampholytes for the separation of protein tryptic digests have been assessed. Three proteins of different molecular masses have been studied: cytochrome C (horse heart), β‐lactoglobulin B (bovine) and human transferrin. Efficient, rapid and repeatable separations of the peptides resulting from the tryptic digestion have been achieved in this buffer. Moreover, the feasibility of the coupling of carrier ampholyte‐based capillary electrophoresis with ESI‐MS has been demonstrated through the study of the cytochrome C tryptic digest.