Primary structure of a chloramphenicol acetyltransferase: Mass spectrometric studies | Zendy

Dell Anne | Zendy; Morris Howard R. | Zendy

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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.

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