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  • Collagenase  (1)
  • Escherichia coli  (1)
  • 1980-1984  (2)
Document type
Keywords
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  • 1980-1984  (2)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Regulation of exoprotease production by temperature and oxygen in Vibrio alginolyticus (1981)
    Springer
    Archives of microbiology 130 (1981), S. 276-280 
    Details
    ISSN: 1432-072X
    Keywords: Collagenase ; Alkaline protease ; Temperature control ; Oxygen control ; Regulation ; Vibrio alginolyticus ; Secretion exoproteins ; Cerulenin ; Quinacrine ; Microbial ecology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The production of an extracellular collagenase and an alkaline protease by Vibrio alginolyticus during stationary phase was inhibited by a temperature shift from 30 to 37°C and by a lack of oxygen. The stability of the exoproteases was unaffected by incubation at 37°C and aeration. The optimum growth temperature for the V. alginolyticus strain was 33.5°C Aeration enhanced the rate of growth of exponential phase cells. Temperature and oxygen did not affect the growth of stationary phase cells when the exoproteases were being produced. Macromolecular synthesis in stationary phase cells was not affected by temperature. There was no rapid release of the exoproteases after temperature shift down and chloramphenicol inhibited the production of the enzymes when added at time of temperature shift down from 37 to 30°C. The regulation of exoprotease production by temperature and oxygen was specific and has implications regarding the ecology of V. alginolyticus. Cerulenin, quinacrine and O-phenanthroline inhibited the production of the exoproteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425940
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Reconstitution of binding protein dependent ribose transport in spheroplasts derived from a binding protein negative escherichia coli K12 mutant and from salmonella typhimurium (1980)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 13 (1980), S. 183-190 
    Details
    ISSN: 0091-7419
    Keywords: reconstitution ; ribose ; transport ; Escherichia coli ; Salmonella typhimurium ; ribose-binding protein ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Highly purified ribose-binding protein from Escherichia coli has been used to reconstitute a binding-protein-dependent ribose transport in spheroplasts derived from a binding-protein-deficient mutant of E coli K 12, and in spheroplasts derived from Salmonella typhimurium. The cross-species reconstitution was nearly as efficient as the reconstitution of the E coli strain from which the binding protein was derived. Antibody raised against the ribose binding protein completely prevented reconstitution, whereas it had no effect on whole cells. The reconstitution procedure has been improved by generating spheroplasts from cells grown in a rich medium and by reducing the background uptake in spheroplasts through a special washing procedure. Rapid purification of ribose binding protein by high pressure liquid chromatography is also described.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400130206
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    Paper (German National Licenses)
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