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  • 2000-2004
  • 1965-1969  (4)
  • 1950-1954
  • 1890-1899
  • 1966  (4)
  • 1898
  • Proteins  (4)
  • 1
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 231-245 
    ISSN: 0570-0833
    Schlagwort(e): Quaternary structure ; Proteins ; Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Many protein molecules, particularly those with high molecular weights, consist not of a single polypeptide chain, but form a complex made up from several polypeptide chains. This structure, which can be reversibly broken down, is known as the quaternary structure. A number of metabolic phenomena can be explained on a molecular basis by invoking the quaternary structure.
    Zusätzliches Material: 9 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 558-566 
    ISSN: 0570-0833
    Schlagwort(e): Casein ; Milk ; Proteins ; Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: 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.
    Zusätzliches Material: 3 Tab.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 798-806 
    ISSN: 0570-0833
    Schlagwort(e): Evolution ; Proteins ; Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The evolution of protein structures is discussed using cytochrome c, hemoglobin, and neurohypophyseal hormones as examples. Although these substances have different biological functions, their evolution is controlled by the same general rules: their primary structures vary at the level of the species, order, or class, but this variation is restricted by the fact that the biological activity of the protein must not be impaired. Alterations (i.e. substitutions, deletions, or additions of amino acid residues) can therefore occur only in certain positions of the peptide chains, although with different frequencies. The total number of alterations thus represents only the final state of a protein and does not take into account successive substitutions which may have taken place at the affected sites. It can therefore give only a rough indication of the phylogenetic distance between two species. The nature of the substituting residues, on the other hand, is a useful guide to zoological cognateness, since it allows the identification of transition molecules which simultaneously contain amino acid residues from the protein of the protein of the evolutionary ancestor and from the protein of the evolutionary descendant.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 807-822 
    ISSN: 0570-0833
    Schlagwort(e): Insulin ; Hormones ; Proteins ; Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The protein hormone insulin occurs widely in the animal kingdom. Although its biological function is always the same, its amino-acid composition varies widely. Insulin consists of two polypeptide chains, which are linked by three cystine residues to form a bicyclic system with a 20-membered and an 85-membered ring. The protein crystallizes in various forms with foreign ions. In solution, insulin normally forms aggregates of 2n molecules. The hormone can be regenerated from the separated polypeptide chains, and its total synthesis has been achieved in a similar manner from synthesized peptide chains. In the biosynthesis of insulin, the two chains are evidently built up separately and subsequently linked together. Insulin promotes the synthesis of glycogen, fat, and protein in the organism; insulin deficiency leads to an increase in the blood-sugar level. At the molecular level, the mechanism of action of the hormone is still unknown. Current hypotheses are discussed. No specific active center has so far been detected in the insulin molecule, which contains several antigenic regions.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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