Release of Penicillinase by Bacillus licheniformis
نویسندگان
چکیده
منابع مشابه
Characteristics of penicillinase release by washed cells of Bacillus licheniformis.
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...
متن کاملFunctional domains of the penicillinase repressor of Bacillus licheniformis.
The penicillinase repressor (PENI) negatively regulates expression of the penicillinase gene (penP) in Bacillus licheniformis by binding to its operators located within the promoter region of penP.penI codes for a protein with 128 amino acids. Filter-binding analyses suggest that the active form of the repressor is a dimer. Genetic analyses of PENI derivatives showed that the repressor carrying...
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Penicillinase was localized in log-phase cells of Bacillus licheniformis 749/C by labeling with ferritin-anti-penicillinase immunoglobulin G conjugate. Mildly fixed homogenized cells, isolated subcellular fractions, and frozen thin sections were labeled. The label was distributed in discrete patches in the cell envelope. The patches extended from the inside part of the membrane to the outside p...
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During membrane-bound penicillinase production, Bacillus licheniformis forms vesicles and tubules that do not appear in the absence of penicillinase production. The major lipids of B. licheniformis were shown to be phospholipids. The proportions, metabolism, and the total phospholipid per cell were shown to be essentially the same in the uninduced control, induced and constitutive penicillinase...
متن کاملBiosynthesis of Bacillus licheniformis penicillinase in Escherichia coli and in Bacillus subtilis.
Modified prepenicillinase was accumulated in both Escherichia coli and Bacillus subtilis treated with globomycin. Although the inhibitions of processings of prepenicillinase and prolipoprotein by globomycin in E. coli are qualitatively similar, they differ in the degree of inhibition at given concentrations of globomycin. The processing of prepenicillinase proceeds much more rapidly in E. coli ...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1967
ISSN: 0022-1287
DOI: 10.1099/00221287-48-2-261