Open AccessBiochemical, immunological and physicochemical comparisons between OHIO‐1 and four SHV‐type β‐lactamases
Author(s) -
Vedel G.,
Paul G.,
Picard B.,
Philippon A.
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03588.x
Subject(s) - klebsiella pneumoniae , isoelectric focusing , isoelectric point , microbiology and biotechnology , beta (programming language) , chemistry , biology , enzyme , biochemistry , escherichia coli , gene , computer science , programming language
The biochemical, immunological and physicochemical properties of the β‐lactamase OHIO‐1 were compared to those of four β‐lactamases commonly found in Klebsiella pneumoniae : SHV‐1, SHV‐3 and the β‐lactamases of strains GN 11‐03 and GN 422. The substrate profile of SHV‐1, OHIO‐1 and of the β‐lactamases GN 11‐03 and GN 422 were similar, while that of SHV‐3 appeared comparable to that of the extended spectrum SHV‐2. Moreover, anti‐TEM‐1 serum inactivated OHIO‐1 as well as SHV‐1 and the β‐lactamases of strains GN 11‐03 and GN 422. Analysis of the electrophoretic mobilities, isoelectric points and titration curves demonstrated that OHIO‐1 and the 4 other β‐lactamases examined were closely related variants. From these findings it appears that OHIO‐1 could be classified among the SHV‐type β‐lactamases.