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  • 1
    Electronic Resource
    Electronic Resource
    Temporary exposure to hydrogen peroxide increases intracellular protein degradation in E. coli (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 44 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A brief exposure of Escherichia coli cells to hydrogen peroxide doubled the rate of intracellular protein degradation. The enhanced protein degradation was energy-dependent. The treatment with hydrogen peroxide caused a transient decrease in the cellular ATP level, but it seems unlikely that the increased rate of proteolysis was caused by starvation or by energy depletion. The findings suggest that a protective mechanism which prevents accumulation of damaged proteins in E. coli cells plays a role in cellular response to oxidative stress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02282.x
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  • 2
    Electronic Resource
    Electronic Resource
    Preparation and properties of an immobilized derivative of penicillinase (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 897-905 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Penicillinase (β-lactamase I, EC 3.5.2.6)secreted by Bacilluus cereus, strain 569/H, was covalently attached to aminoethyl cellulose via glutaraldehyde. The immobilized derivative shows increased thermostability and decreased susceptibility to conformational changes induced by certain substrates of penicillinase. The decline in the rate of such substrates was consequently suppressed by immobilization. A marked increase in Km was observed with all substrates except for the unsubstituted 6-aminopenicillanic acid. The altered properties of the new derivative are attributed to the constraint imposed by immobilization on the conformational flexibility of the enzyme molecule. Thus, apart from obvious technological interest, immobilized penicillinase provides a useful model for the study of the role of flexibility in the function of an enxyme.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210512
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    Paper (German National Licenses)
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