| Localization of cell-bound penicillinase in Bacillus licheniformis. | |
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MedLine Citation:
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PMID: 4302175 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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When protoplasts are prepared from Bacillus licheniformis (strain 749/C, constitutive for penicillinase), approximately 60% of the cell-bound penicillinase is released. The remainder is retained by the protoplast and cannot be removed by washing. This release is specific, in that less than 7% of the cellular reduced nicotinamide adenine dinucleotide (NADH) dehydrogenase and alpha-glucosidase is liberated by the treatment. The freed penicillinase is excluded from G-200 Sephadex, and it is partially sedimented with a force of 65,000 x g for 20 hr. It is probably attached to characteristic tubular and vesicular structures with single-layered membranes that are comparable to structures previously described in intact penicillinase-forming cells. The specific activity of the organelle is more than six times that of twice washed peripheral membrane; furthermore, about 8% of the protein of the structure is penicillinase. At substrate concentrations (benzylpenicillin) of about one-fifth the K(m) value, whole cells show a slight permeability restriction, although this does not occur in isolated particles and protoplasts. |
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Authors:
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M G Sargent; B K Ghosh; J O Lampen |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Journal of bacteriology Volume: 96 ISSN: 0021-9193 ISO Abbreviation: J. Bacteriol. Publication Date: 1968 Oct |
Date Detail:
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Created Date: 1969-02-01 Completed Date: 1969-02-01 Revised Date: 2010-09-10 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 1329-38 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Bacillus
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cytology*,
enzymology* Cytoplasm / analysis Glucosidases / metabolism NAD / metabolism Penicillinase* / analysis, isolation & purification Protoplasts / cytology, enzymology |
| Chemical | |
Reg. No./Substance:
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53-84-9/NAD; EC 3.2.1.-/Glucosidases; EC 3.5.2.-/Penicillinase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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