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  • 1965-1969  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Lysozymes characterized in Duck Egg-white: Isolation of a Histidine-less Lysozyme (1965)
    [s.l.] : Nature Publishing Group
    Nature 208 (1965), S. 1204-1205 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] One 1. of duck egg-white was homogenized with 4 1. of water; the pH was adjusted to 4-5 and the solution was mixed for 4 h with 200 ml. of 'Amberlite CG-50 (Type II)' buffered at pH 6-5 with a 0-2 M phosphate buffer. The purification was continued following the procedure of Jolles et al.2: elution ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2081204a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Arthritogenicity and protective effect against adjuvant arthritis of wax DS fractions (glycolipids without a nitrogen-containing moiety) ofMycobacterium tuberculosis var.hominis andbovis (1968)
    Springer
    Cellular and molecular life sciences 24 (1968), S. 716-717 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Résumé Les cires DS des Mycobactéries (souches humaines et bovines), glycolipides dépourvus de la partie azotée présente dans les cires DP, ne provoquent pas d'arthrite chez le rat; contrairement aux cires DP acétylées, elles ont un effet protecteur vis-à-vis d'une cire DP arthrogène seulement si elles sont injectées 40 jours avant cette dernière.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02138335
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Lysozyme: Ein Kapitel Molekularbiologie (1969)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 81 (1969), S. 244-256 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Hühnereiweiß-Lysozym war das erste Enzym, dessen Tertiärstruktur aufgeklärt werden konnte. Seine Peptidkette ist in zwei etwa gleich großen Teilen angeordnet, zwischen denen ein tiefer Spalt klafft. Die Substrate (und Inhibitoren) werden in diesem Spalt durch Wasserstoffbrücken gebunden und unter Mitwirkung von Glu 35 und Asp 52  -  die das aktive Zentrum bilden  -  hydrolysiert.  -  Die Lysozyme, die in vielen Tier- und Pflanzenarten vorkommen, sind zwar chemisch verschieden, haben jedoch qualitativ die gleiche biologische Aktivität; quantitativ lassen sich große Unterschiede nachweisen, die auch die Spezifität betreffen. Nach Infektion mit Bakteriophagen entsteht in E. coli ein Lysozym, dessen Bildung von der Phagen-DNS kontrolliert wird. Da mutierte Phagen abgeänderte Lysozyme erzeugen, eröffnet sich ein weites Feld für die molekularbiologische Forschung.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19690810703
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  • 4
    Electronic Resource
    Electronic Resource
    Progress in the Chemistry of Casein (1966)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 558-566 
    Details
    ISSN: 0570-0833
    Keywords: Casein ; Milk ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Casein from cow's milk is not a single substance, but can be resolved into numerous components. These include x-casein, which is the only fraction that contains appreciable quantities of sugars. This component plays a very important role in the clotting of milk by rennin, when it is split into an almost sugar-free fraction, para-x-casein, and a fraction containing sugars, x-caseinoglycopeptide. Caseinoglycopeptides have been isolated not only from the casein of cow's milk, but also from the caseins of sheep. Goat, and human milk. The second part of the paper deals with the clotting of milk by rennin and the amino acid sequence in caseinoglycopeptides.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.196605581
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  • 5
    Electronic Resource
    Electronic Resource
    Lysozymes: A Chapter of Molecular Biology (1969)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 8 (1969), S. 227-239 
    Details
    ISSN: 0570-0833
    Keywords: Lysozymes ; Enzymes ; Tertiary structure ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Hen egg-white lysozyme was the first enzyme whose tertiary structure could be elucidated. The peptide chain of this enzyme is arranged in two sections, of approximately equal size, that are separated by a deep cleft. Substrates (and inhibitors) are bound in this cleft via hydrogen bonds and are hydrolyzed under the action of Glu 35 and Asp 52, which form the active site of the enzyme. Although the lysozymes, which occur in many species of animals and plants, exhibit differences in their chemical behavior, they have the same qualitative biological activity; quantitatively important differences have been noted which also concern the specificity. Infection of E. coli with bacteriophages gives rise to a lysozyme whose formation is controlled by the phage DNA. The fact that mutated lysozymes are produced when the phages are treated with mutagens opens new fields of research in molecular biology.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.196902271
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