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Primary structure of a chloramphenicol acetyltransferase: Mass spectrometric studies
Author(s) -
Dell Anne,
Morris Howard R.
Publication year - 1981
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.1200080310
Subject(s) - chloramphenicol acetyltransferase , protein primary structure , subtilisin , chemistry , acetyltransferase , fragmentation (computing) , mass spectrometry , chromatography , peptide , peptide sequence , chloramphenicol , elastase , biochemistry , enzyme , biology , antibiotics , ecology , gene expression , promoter , acetylation , gene
Low resolution electron impact mass spectrometry has been used as a major tool in the sequencing of a chloramphenicol acetyltransferase (mol. wt 25 668). Mass spectrometric data from mixtures of peptides from elastase, chymotryptic and subtilisin digests have defined 83% of the protein sequence. Several, previously unrecognized, peptide fragmentation pathways are reported.