نتایج جستجو برای: penicillinase

تعداد نتایج: 945  

Journal: :Antimicrobial agents and chemotherapy 1974
P J Lawrence

Benzylpenicillin inhibits the development of the forespore septum in sporulating Bacillus megaterium cells. The inhibitory effect is a function of the duration of exposure to the antibiotic and is completely reversible by penicillinase. Under the incubation conditions employed, less than 20% of the covalently bound antibiotic is released from the cells. The penicillin which remains bound to the...

Journal: :The British journal of venereal diseases 1983
T O Odugbemi S T Brown J Biddle S Johnson G Perkins W DeWitt W L Albritton

The plasmid patterns of 90 isolates of Neisseria gonorrhoeae (including 39 penicillinase-producing strains) originating from various countries in Africa were determined. Serogrouping by coagglutination and auxotyping were used to characterise the isolates. The 4.4-megadalton plasmid was present in seven isolates out of 39 penicillinase-producing strains, two of which occurred with a conjugative...

Journal: :The Biochemical journal 1958
M R POLLOCK M KRAMER

Journal: :Journal of clinical pathology 1968
J H Hewitt M T Parker

Twenty-eight penicillinase-forming cultures of Staphylococcus aureus and their penicillinase-negative variants were examined for resistance to benzylpenicillin, methicillin, cephalothin, and cephaloridine. The results supported the view that cephaloridine was more easily destroyed by staphylococcal penicillinase than was cephalothin. In our tube-dilution tests, the minimum inhibitory concentrat...

Journal: :The Biochemical journal 1967
N W Coles R Gross

1. Growth of Staphylococcus aureus (8325; alphai(-)p(+)), constitutive for the production of penicillinase, in CY medium results in about 40% of the enzyme being free in the medium. By modifying the medium, 98% of the enzyme remains cell-bound. 2. Part of this is bound ionically to the surface of the cell wall and may be liberated instantaneously by certain inorganic anions. Maximum liberation ...

Journal: :Journal of bacteriology 1968
M G Sargent B K Ghosh J O Lampen

Saline-washed cells of Bacillus licheniformis strain 749/C (constitutive for penicillinase) were able to release exopenicillinase in the presence of concentrations of chloramphenicol that prevented protein synthesis completely. The release reaction was strongly pH-dependent, occurring at a faster rate at alkaline pH in anionic or cationic buffers than at neutral pH. A strongly pH-dependent rele...

Journal: :Journal of Bacteriology 1957

Journal: :Memorias do Instituto Oswaldo Cruz 2003
Rafael Llanes Miriam González Isabel Martínez Jorge Sosa Daymi Guzmán Oderay Gutiérrez Alina Llop Lizet Sánchez

Four methods (chromogenic, acidimetric, inhibition, and iodometric) for demonstration of the beta-lactamase production by 70 isolates of Neisseria gonorrhoeae, were evaluated in Cuba. There was 100% correlation between all beta-lactamase methods and the standardized penicillin dilution susceptibility test for penicillinase-non-producing N. gonorrhoeae. For penicillinase-producing N. gonorrhoeae...

Journal: :Journal of clinical microbiology 2014
Lito E Papanicolas Jan M Bell Ivan Bastian

Recent studies have shown that chromogenic cephalosporin tests are inferior to disc zone edge tests in detecting penicillinase in Staphylococcus aureus isolates, resulting in a change to CLSI and EUCAST guidelines in 2012. We sought to confirm these findings using Australian isolates and compare the performance of the CLSI and EUCAST methods, which use different disc strengths, penicillin at 10...

Journal: :Journal of bacteriology 1965
E J Benner J V Bennett J L Brodie W M Kirby

Benner, Ernest J. (University of Washington School of Medicine, Seattle), John V. Bennett, Jean L. Brodie, and William M. M. Kirby. Inactivation of cephalothin and cephaloridine by Staphylococcus aureus. J. Bacteriol. 90:1599-1604. 1965.-Marked differences were observed in the susceptibility of penicillinase-producing staphylococci to cephalothin and cephaloridine. All of 100 strains of penicil...

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