Partial Characterization of a Beta-Lactamase from
            <i>Vibrio parahaemolyticus</i>
            by a New Automated Microiodometric Technique

DeBell, Robert M.; Hickey, Thomas M.; Uddin, David E.

doi:10.1128/aac.13.2.165

Cited by 6 publications

(3 citation statements)

References 21 publications

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“…Laboratories having a spectropho- fast analyzer can achieve great accuracy by rapid replicate analysis similar to that reported here and earlier by DeBell et al (4). The latter investigators adapted the microiodometric method to a Rotochem and reported excellent enzyme kinetic results for a Vibrio parahaemolyticus beta-lactamase (4). PADAC can also be used as the beta-lactamlabile substrate for inhibition studies (6a, 7).…”

Section: Discussionmentioning

confidence: 99%

In vitro evaluation of pyridine-2-azo-p-dimethylaniline cephalosporin, a new diagnostic chromogenic reagent, and comparison with nitrocefin, cephacetrile, and other beta-lactam compounds

Jones¹,

Wilson²,

Novick³

1982

J Clin Microbiol

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azo-p-dimethylanaline cephalosporin (PADAC), a chromogenic reagent which is purple and changes to yellow upon cleavage of its beta-lactam ring, was evaluated in comparison with other chromogenic cephalosporins. PADAC exhibited little antimicrobial activity against gram-negative bacteria, but did have good activity (minimum inhibitory concentration, 0.12 to 0.5 ,ug/ml) against Staphylococcus aureus, a quality comparable to nitrocefin. Nitrocefin, however, demonstrated an unexpected and uniquely potent activity against Streptococculs faecalis (minimum inhibitory concentration,-0.06 to 0.12 p.g/ml). The relative hydrolysis rate of PADAC when subjected to six different beta-lactamases was substantially greater than that of cephacetrile, but less than that of nitrocefin. The relative hydrolysis rates of PADAC and nitrocefin were comparable with type Illa beta-lactamase and that derived from Bacillus cereus. The inhibition of betalactamase hydrolysis of the chromogenic cephalosporin substrates by six enzymestable inhibitors was generally greater with PADAC than with nitrocefin. Unlike nitrocefin, PADAC mixed with 50% human serum or various broth culture media showed no evidence of color change or degradation over several hours. The subsequent enzyme hydrolysis rates of such mixtures were the same as in phosphate buffer. Beta-lactamase-containing bacterial suspensions and clinical specimens containing such bacteria produced positive visual and spectrophotometric color changes when mixed with PADAC or nitrocefin. Although color changes occurred more slowly with PADAC than with nitrocefin, PADAC was not adversely influenced (non-enzyme-related color change) by the protein content of specimens. PADAC appears to be a promising alternative for betalactamase diagnostic testing in the clinical and research microbiology laboratory.

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Section: Discussionmentioning

confidence: 99%

In vitro evaluation of pyridine-2-azo-p-dimethylaniline cephalosporin, a new diagnostic chromogenic reagent, and comparison with nitrocefin, cephacetrile, and other beta-lactam compounds

Jones¹,

Wilson²,

Novick³

1982

J Clin Microbiol

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“…AGENTS CHEMOTHER. (4), Citrobacter (unidentified species [10]), Enterobacter gergoviae (2), E. sakazakii (5), Klebsiella ozaenae (6), K. rhinoscleromatis (3), Providencia alcalifaciens (2), Serratia liquefaciens (5), S. rubidaea (2), and Yersinia enterocolitica (4). (12), P. fluorescens-putida (8), P. putrefaciens (1), P. stutzeri (18), P. acidovorans (3), P. alcaligenes (6), P. paucimobilis (1), P. testosteroni (5) and Pseudomonas sp.…”

mentioning

confidence: 99%

Cefotetan, a new cephamycin: comparison of in vitro antimicrobial activity with other cephems, beta-lactamase stability, and preliminary recommendations for disk diffusion testing

Ayers¹,

Jones²,

Barry³

et al. 1982

Antimicrob Agents Chemother

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Cefotetan is a new, potent, 7a-methoxy cephalosporin (cephamycin). The in vitro activity of cefotetan tested in a multiphasic, collaborative study against 12,260 consecutive clinical isolates and 448 selected isolates showed 93% of Enterobacteriaceae, 90% of methicillin-susceptible Staphylococcus aureus (broth dilution), 83% of Bacteroides fragilis, and 72% of non-enterococcal streptococci to be inhibited by s8 ,ug/ml. ,B-Lactamase-producing and -nonproducing Haemophilus influenzae strains were inhibited by s1.0 ,ug/ml. Cefotetan's inhibitory spectrum paralleled those of the newest generation of cephems and exceeded those of cefoxitin and cefamandole. No useful activity was present against Streptococcus faecalis or Pseudomonas aeruginosa. Cefotetan was bactericidal without significant inoculum effect and was highly resistant to hydrolysis by Richmond-Sykes types I, III, and IV P-lactamases. Hydrolysis of the chromogenic cephalosporin PADAC (pyridine-2-azo-p-dimethylaniline cephalosporin) by type I ,B-lactamases was markedly inhibited by concentrations of cefotetan similar to those of the potent inhibitor dicloxacillin. Analysis of agar disk diffusion for several disk potencies and broth dilution susceptibility tests by regression and error rate-bounding methods produced preliminary tentative zone standards (30-,ug disk, using minimal inhibitory concentration breakpoints of <8 p.g/ml susceptible and >32 ,ug/ml resistant, or 75-,ug disk, using minimal inhibitory concentration breakpoints of <16 ,ug/ml susceptible and -64 ,ug/ml resistant) of .18 mm susceptible, s14 mm resistant, and 15 to 17 mm indeterminate. Staphylococcus aureus testing with the 30-,ug disk is not recommended.

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“…Only one strain, V. alginolyticus 7608, possessed unusually high SOD levels. Although we have no direct explanation for this phenomenon, we have noted that this strain synthesizes higher amounts of other enzymes, such as ,8-lactamases, than the other vibrios (9).…”

Section: Resultsmentioning

confidence: 72%

Superoxide dismutase and catalase levels in halophilic vibrios

Daily¹,

DeBell²,

Joseph³

1978

J Bacteriol

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Superoxide dismutase (SOD) and catalase (CAT) levels were determined for several aerobically grown halophilic vibrios and compared with those found in aerobically grown Escherichia coli K-12. The SOD levels ranged from 25 to 103.6 U/mg of protein for the vibrios compared with 44.6 U/mg of protein for E. coli. The CAT levels ranged from 2.1 to 32.1 U/mg of protein. Electrophoretic analysis of cell extracts revealed that the halophilic vibrios tested possessed only one detectable SOD enzyme, except one strain which possessed two distinct enzymes, as compared with the three SOD enzymes in aerobically grown E. coli K-12. A comparison of anaerobically and aerobically grown vibrios revealed a threeto fourfold increase in SOD activity in the aerobic cells, suggesting that oxygen acts as an inducer for SOD in the vibrios as has been reported for E. coli. In one strain, Vibrio parahaemolyticus 27519, both SOD enzymes were observed in low levels in anaerobic and at higher levels in aerobically grown cells as compared with only one SOD enzyme in anaerobically grown E. coli. This suggests that differences in SOD regulation occur between the two genera. Our results indicate that halophilic vibrios possess SOD, which could enhance virulence by allowing the organisms to survive in oxygenated environments. 161:395-401.

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Partial Characterization of a Beta-Lactamase from Vibrio parahaemolyticus by a New Automated Microiodometric Technique

Cited by 6 publications

References 21 publications

In vitro evaluation of pyridine-2-azo-p-dimethylaniline cephalosporin, a new diagnostic chromogenic reagent, and comparison with nitrocefin, cephacetrile, and other beta-lactam compounds

In vitro evaluation of pyridine-2-azo-p-dimethylaniline cephalosporin, a new diagnostic chromogenic reagent, and comparison with nitrocefin, cephacetrile, and other beta-lactam compounds

Cefotetan, a new cephamycin: comparison of in vitro antimicrobial activity with other cephems, beta-lactamase stability, and preliminary recommendations for disk diffusion testing

Superoxide dismutase and catalase levels in halophilic vibrios

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