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  • 2020-2023
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  • Proteins
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  • 2020-2023
  • 1985-1989
  • 1970-1974  (4)
  • 1965-1969  (4)
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  • 1
    ISSN: 1432-1440
    Keywords: Lymph ; Proteins ; Immunoglobulins ; Isoenzymes ; Peptides ; Lymphe ; Proteine ; Immunglobuline ; Isoenzyme ; Peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Die Proteine aus Ductus thoracicus-Lymphe von 7 Patienten mit Lebercirrhose wurden mit Blutseren derselben Patienten sowie mit Lymph- und Blutseren von Normalpersonen nach Konzentration, elektrophoretischem Verhalten im Polyacrylamidgel, immunologischen Eigenschaften und Enzymgehalt verglichen. Auffallend war in den Lymphseren ein relativ geringer IgM-Gehalt, ein teilweise erhöhter IgA-Gehalt, eine hohe Albuminkonzentration, ein lebertypisches LDH-Isoenzymmuster, in 2 Lymphseren das Vorkommen eines lebereigenen Proteins und in einigen pathologischen Lymphseren das Auftreten eines Glykopeptids in hoher Konzentration.
    Notes: Summary The proteins of the thoracic duct lymph and blood serum from seven patients with liver cirrhosis and from normal persons were characterized by protein determination, electrophoresis on polyacrylamid gel, as well as by immunological and enzymatic methods. Differences between lymph and blood sera were observed. The lymph sera showed a low IgM content, a partially elevated IgA content, high albumin concentration, and altered LDH-isoenzyme pattern. In some lymph sera high concentrations of soluble protein from the liver and a glycopeptide were found.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 129 (1972), S. 56-64 
    ISSN: 1432-0878
    Keywords: Liver regeneration ; Membranes ; Nucleic acids ; Proteins ; Solubility ; Biochemical analysis and electronmicroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Prior to the onset of mitotic activity in the regenerating mouse liver, the concentrations of total protein and DNA, but not of RNA, decreased to 93 per cent of their levels in normal liver. During maximum mitosis (48–72 hours), the DNA and RNA concentrations were 110 per cent of their normal levels. The concentrations of liver nucleic acids 24 hours after a sham-operation were also about 110 per cent of normal values. Increased concentrations of insoluble protein were found at 12, 24 and 144 hours after partial hepatectomy. This may reflect an increase in the stability of the liver cell membranes during the regenerative period. Increased amounts of various cytoplasmic membranes were indicated by electronmicroscopy and may also have contributed to the increase in insoluble protein. A temporary increase in the measured solubility of the liver protein occurred during maximum mitosis. It is suggested that this was due to the association of protein with lipids during the depletion of accumulated fat from the regenerating liver.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 11 (1972), S. 883-893 
    ISSN: 0570-0833
    Keywords: Gene expression ; Translation of genetic information ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: During transcription, genetic information is transferred from DNA to mRNA, the process being catalyzed by DNA-dependent RNA polymerase. Transcription comprises binding of the RNA polymerase to DNA, initiation, elongation, and termination. The interplay of the positive and negative control elements of these processes is illustrated for bacteria and bacteriophages.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 11 (1972), S. 894-906 
    ISSN: 0570-0833
    Keywords: Cooperative phenomena ; Conformation analysis ; Proteins ; Rearrangement ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In globular proteins, the complicated steric arrangement of the polypeptide chain is determined by several interdependent cooperative interactions. These macromolecules are capable of reacting to changes in the environmental conditions such as temperature and pressure or the concentration of a wide range of compounds by changing their conformation and hence their biological and chemical properties. They are thus suitable for regulation processes or information storage in solution with a wide range of time constants. Environmental effects of this kind can be followed and explained in part at the molecular level by investigation of the time-dependent reversible unfolding of a number of proteins that can be described to a good approximation by a strongly cooperative “all-or-none” transition between two states.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 231-245 
    ISSN: 0570-0833
    Keywords: Quaternary structure ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 558-566 
    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
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  • 7
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 798-806 
    ISSN: 0570-0833
    Keywords: Evolution ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 807-822 
    ISSN: 0570-0833
    Keywords: Insulin ; Hormones ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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