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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Journal of industrial microbiology and biotechnology 5 (1990), S. 59-64 
    ISSN: 1476-5535
    Schlagwort(e): Cellulase ; Endoglucanase ; Cellulose ; Pseudomonas
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary The recombinant plasmid, pPFC4, which carriesPseudomonas fluorescens subsp.cellulosa chromosomal DNA was previously isolated on the basis of its ability to direct the expression of endoglucanase inEscherichia coli. In the present study, some physical and chemical properties of this activity were characterized. The major portion (78.4%) of the endoglucanase activity is found in the periplasmic space ofE. coli. This plasmid-encoded endoglucanase has a pH optimum of approximately 6.0 and a temperature optimum of approximately 50°C. With carboxymethylcellulose-zymograms, after polyacrylamide gel electrophoresis, periplasmic extracts fromE. coli carrying pPFC4 show six distinct bands with endoglucanase activity. The molecular mass of the major endoglucanase band is approximately 29 kDa while the remaining bands with endoglucanase activity range from 48 to 100 kDa. Although the basis of this heterogeneity is not known, the DNA insert of pPFC4 that encodes endoglucanase activity is not large enough to contain six separate genes; hence, the observed array of endoglucanases may result from post-translational modification of one or two primary gene products.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Journal of industrial microbiology and biotechnology 1 (1987), S. 277-282 
    ISSN: 1476-5535
    Schlagwort(e): Recombinant DNA ; Gene expression ; Genetic engineering ; Biotechnology
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary A variety of factors affect the expression of foreign proteins inEscherichia coli. These include: promoter strength, efficiency of ribosome binding, stability of the foreign protein inE. coli, location of the foreign protein inE. coli, the codons used to encode the foreign protein, the metabolic state of the cell, and the location, stability and copy number of the foreign gene. This paper contains a critical review of these factors with the idea that a detailed understanding of them is the key to the development of strategies for the efficient large-scale production of foreign proteins inE. coli.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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