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The determination of sequence information in homologously related proteins by mass spectrometry
Author(s) -
Dell Anne,
Morris Howard R.,
Williams Dudley H.,
Ambler Richard P.
Publication year - 1974
Publication title -
biomedical mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0306-042X
DOI - 10.1002/bms.1200010411
Subject(s) - cyanogen bromide , azurin , mass spectrometry , chemistry , peptide , protein sequencing , peptide sequence , pseudomonas fluorescens , residue (chemistry) , biochemistry , bacteria , chromatography , biology , copper , organic chemistry , genetics , gene
An azurin, a small respiratory copper protein from the bacterium Pseudomonas fluorescens biotype G, has been studied by mass spectrometry to determine sequence information. The study of homologously related proteins by mass spectiometry is particularly attractive, since the correct nature of major parts of the deduced sequences can be confirmed by comparison with the sequences of the protein from related organisms. An oxidized tryptohan residue has been identified amongst the products from a cyanogen bromide digest of this wild type azurin. In the same digest, a product is also found to arise from cleavage of the peptide chain at the C‐terminal side of the same tryptophan residue. These results are rationalized.