Premium
Drug Resistance of Enteric Bacteria
Author(s) -
Sawai Tetsuo,
Mitsuhashi Susumu,
Yamagishi Saburo
Publication year - 1968
Publication title -
japanese journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0021-5139
DOI - 10.1111/j.1348-0421.1968.tb00415.x
Subject(s) - proteus mirabilis , microbiology and biotechnology , proteus , serratia , klebsiella pneumoniae , bacteria , providencia , escherichia coli , proteus vulgaris , biology , enterobacteriaceae , strain (injury) , staphylococcus aureus , pseudomonas , biochemistry , anatomy , gene , genetics
The strains of gram‐negative rod bacteria which are resistant to α‐aminobenzylpenicillin and do not harbor the R factors were selected from our stock cultures of clinical origin. It was found that all strains produced β‐lactamases which are species‐specific in their substrate profiles and classified into three groups; 1) Typical cephalosporinase in the strains of Escherichia freundii, Aerobacter aerogenes, Arizona, Proteus morganii, Proteus rettgeri, Proteus inconstans and a strain GN633 of the Serratia group. 2) Cephalosporinase in the strains of Proteus vulgaris and a strain GN629 of the Serratia group, which has a property of penicillinase to some extent. 3) Penicillinase in the strains of Escherichia coli, Klebsiella pneumoniae and Proteus mirabilis . It was found that cephalosporinase was generally inducible enzyme, penicillinase was constitutive, and the penicillinase synthesized by the strains carrying R factors belonged to the third group. Penicillinases of two R factors, RGN14 and RGN238 which were isolated in this laboratory and belonged to the penicillinase of the third group, were studied by comparing their substrate profiles and immunological properties. It was demonstrated that penicillinases of RGN14 and RGN238 differed each other, while the penicillinase of K. pneumoniae was quite similar to that of RGN14 both enzymologically and immunologically.