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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 30 (1974), S. 1407-1409 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung In Ribosomen von Klapperschlangenleber ist das Verhältnis RNS/Protein 0,96, und das Molekulargewicht der meisten ribosomalen Proteine liegt zwischen 10 und 45×103 Daltons. Das durchschnittliche Molekulargewicht ist 22000 bzw. 26000 Daltons für die Proteine der 40 S bzw. der 60 S Untereinheit. Diese Daten weisen darauf hin, dass der erhöhte Proteingehalt der Ribosomen dieses Reptils gegenüber Ribosomen von Bakterien durch das Vorhandensein von Proteinen mit höherem Molekulargewicht beding ist.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 29 (1973), S. 37-39 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Résumé Nous avons étudié la distribution du RNA 5S dans le foie du serpent sud-américainCrotalus durissus terrificus. Nos résultats ont montré que le RNA 5S de ce reptile est associé à la sous-unité ribosomique 60 S. D'autre part, la mobilité electrophorétique de ce RNA de faible poids moléculaire est la même que celle d'Escherichia coli et de pupe d'Apis mellifera L.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 19 (1999), S. 157-161 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A xylanase was removed from crude extract of the fungus Penicillium janthinellum under optimized conditions: 0.10M phosphate buffer, pH 7.0, 0.2 M BDBAC (N-benzyl-N-dodeceyl-N-bis (2-hydroxyethyl) ammonium chloride), 7.5% hexanole, 30°C and an agitation time of 1 minute. At 1.42 mg per ml protein concentration, 73% of the xylanase activity was recovered and a 7-fold enrichment factor was obtained. The enzyme had a molecular weight (MW) of 20.1 kDa and the isoelectric point (PI) revealed the presence of two protein bands with a PI of 6.0 and 6.5. The optimum pH and optimum temperature were 4.2 and 50°C, respectively. The low pH differential between the aqueous medium and the protein PI seemed to influence the xylanase transportation into the reversed micelles.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
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