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  • 1990-1994  (3)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 5 (1991), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The rate of folding of the precursor of β-lactamase is not influenced by the presence of SecB under conditions in which GroEL/ES retards the folding. Wild-type β-lactamase and several mutants in the signal or the mature protein, affecting either transport or enzyme kinetics and probably folding, were examined for total expression, total enzymatic activity, and transported β-lactamase (in vivo resistance) in secB- and secB+ strains. We conclude that there is no indication of any relevant interaction between SecB and pre-β-lactamase in vitro, nor did the secB- mutation affect the transport of wild–type β-lactamase or any of the mutants in vivo. Thus, putative Escherichia coli‘folding modulators’must be of limited specificity.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 347 (1990), S. 497-498 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE use of E. coli as an expression host brings the arsenal of bacterial gene technology to antibody molecules. The ease with which E. coli can be manipulated greatly facilitates antibody engineering of both the antigen binding pocket and the framework. The efficient transformation and transfection ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 11 (1991), S. 449-456 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The production of genetically engineered antibodies in Escherichia coli is now possible. The resulting fragments are completely functional and have antigen binding constants industinguishable from the natural antibody. This article summarizes the biochemical basis of this newly developed technology and the properties of the resulting fragments. It is likely that this technology will have an important role in antibody production for technical, medical and research uses. Screening of E. coli libraries may mount a challenge to traditional antibody production methods.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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