| Localization of alkaline phosphatase in three gram-negative rumen bacteria. | |
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MedLine Citation:
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PMID: 4147649 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Of the three species (Bacteroides ruminicola, B. succinogenes, and Megasphaera elsdenii) of anaerobic gram-negative rumen bacteria studied, only B. ruminicola produced significant amounts of alkaline phosphatase. This enzyme, which is constitutive, showed a greater affinity for p-nitrophenylphosphate than for sodium-beta-glycerophosphate and was shown to be located exclusively in the periplasmic space of log-phase cells. Small amounts of this enzyme were released from these cells in stationary-phase cultures, but washing in 0.01 M MgCl(2) and the production of spheroplasts by using lysozyme in 0.01 M MgCl(2) did not release significant amounts of the enzyme. Exposure to 0.2 M MgCl(2) did not release significant amounts of the periplasmic alkaline phosphatase of the cell, and when these cells were spheroplasted with lysozyme in 0.2 M MgCl(2) only 25% of the enzyme was released. Spheroplasts were formed spontaneously in aging cultures of B. ruminicola, but even these cells retained most of their periplasmic alkaline phosphatase. It was concluded that the alkaline phosphatase of B. ruminicola is firmly bound to a structural component within the periplasmic area of the cell wall and that the enzyme is released in large amounts only when the cells break down. The behavior of alkaline phosphatase in this bacterium contrasts with that of conventional periplasmic enzymes of aerobic bacteria, which are released upon conversion into spheroplasts by lysozyme and ethylenediaminetetraacetic acid and by other types of cell wall damage. All three species of bacteria studied here, as well as bacteria found in mixed populations in the rumen, have thick, complex layers external to the double-track layer of their cell walls. In addition, B. ruminicola produces a loose extracellular material. |
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Authors:
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K J Cheng; J W Costerton |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Journal of bacteriology Volume: 116 ISSN: 0021-9193 ISO Abbreviation: J. Bacteriol. Publication Date: 1973 Oct |
Date Detail:
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Created Date: 1973-12-16 Completed Date: 1973-12-16 Revised Date: 2009-11-18 |
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: 424-40 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Alkaline Phosphatase
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biosynthesis,
isolation & purification*,
metabolism Anaerobiosis Animals Bacteria / enzymology* Bacteroides / enzymology* Cell Wall / enzymology Cell-Free System Glutamate Dehydrogenase / metabolism Magnesium Microscopy, Electron Microscopy, Phase-Contrast Muramidase NADH, NADPH Oxidoreductases / metabolism Rumen / microbiology* Species Specificity Spectrophotometry Spheroplasts / enzymology Vibration |
| Chemical | |
Reg. No./Substance:
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7439-95-4/Magnesium; EC 1.4.1.2/Glutamate Dehydrogenase; EC 1.6.-/NADH, NADPH Oxidoreductases; EC 3.1.3.1/Alkaline Phosphatase; EC 3.2.1.17/Muramidase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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