Open AccessImmunological comparison between OXA-2 beta-lactamase and those mediated by other R plasmids
Author(s) -
Susan Holland,
Jeremy W. Dale
Publication year - 1985
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.27.6.989
Subject(s) - plasmid , beta (programming language) , homology (biology) , enzyme , gene , sequence homology , beta lactamase , biology , microbiology and biotechnology , antibody , genetics , chemistry , peptide sequence , biochemistry , escherichia coli , computer science , programming language
Antibodies to the OXA-2 beta-lactamase inhibited both OXA-2 and OXA-3 enzymes, but there was no effect on any other beta-lactamase. The cross-neutralization indicates considerable homology between the OXA-2 and OXA-3 enzymes and supports the suggestion that the OXA-3 beta-lactamase may have been derived from the OXA-2 gene via a deletion.