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Purification and Some Properties of β‐Lactamases from Proteus rettgeri and Proteus inconstans
Author(s) -
Ohya Satoshi,
FujiiKuriyama Yoshiaki,
Yamamoto Mitsuyo,
Sugawara Shinichi
Publication year - 1980
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1980.tb02886.x
Subject(s) - isoelectric point , proteus , isoelectric focusing , biology , enzyme , microbiology and biotechnology , antiserum , bacteria , polyacrylamide gel electrophoresis , biochemistry , cefoxitin , escherichia coli , antibody , genetics , immunology , staphylococcus aureus , gene
Two β‐lactamases were isolated from strains of Proteus species and purified, one from a strain of P. rettgeri and the other from a strain of P. inconstans . Each enzyme preparation gave a single protein band on polyacrylamide gel electrophoresis. Molecular weights of P. rettgeri and P. inconstans enzymes were found to be 42,000 and 43,000, and their isoelectric points pH 8.7 and 8.6, respectively. The two enzymes presented typical cephalosporinase profiles. Cefmetazole (CS‐1170) and cefoxitin, both cephamycin antibiotics, not only resisted hydrolysis by both of the enzymes, but also inhibited their activities competitively. Rabbit antiserum against purified P. rettgeri enzyme inhibited the activity of both purified and crude enzyme preparations from other strains of P. rettgeri so far tested. None of the β‐lactamases produced by other species of Proteus including P. inconstans was inhibited by the antiserum, thus showing that the purified cephalosporinase was of the species‐specific type. The enzymological properties of the preparations were compared with those of β‐lactamases derived from other gram‐negative enteric bacteria.