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Comparison of peptide analysis results for horse, bovine and dog cytochrome c using capillary electrophoresis/mass spectrometry with untreated capillary column and basic buffer condition
Author(s) -
Takada Yasuaki,
Nakayama Kanae,
Yoshida Motoko,
Sakairi Minoru
Publication year - 1994
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290080906
Subject(s) - chemistry , chromatography , capillary electrophoresis , peptide , mass spectrometry , cytochrome c , horse , capillary electrophoresis–mass spectrometry , capillary action , amino acid , biochemistry , mitochondrion , electrospray ionization , paleontology , materials science , composite material , biology
Peptide analysis of cytochrome c using capillary electrophoresis/mass spectrometry was demonstrated to be a rapid, sensitive and useful technique for providing information concerning the location of variation. We analyzed tryptic digests of horse, bovine and dog cytochrome c , and compared the peptide analysis results for information concerning amino acid sequences in proteins. The differences in amino acid sequence were confirmed by taking into consideration that all the other fragments are identical in each map. The use of an untreated capillary column with basic buffer condition (water+acetonitrile+(20 g/L) ammonium carbonate (70/20/10), pH 9.2) had a reproducibility of migration times to within about 2%.