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  • 1965-1969  (7)
  • 1890-1899
  • 1870-1879
  • 1966  (7)
  • 1899
  • 1877
  • Proteins  (4)
  • Flexor reflex afferents  (3)
Materialart
Erscheinungszeitraum
  • 1965-1969  (7)
  • 1890-1899
  • 1870-1879
Jahr
  • 1966  (7)
  • 1899
  • 1877
  • 1967  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Experimental brain research 1 (1966), S. 306-319 
    ISSN: 1432-1106
    Schlagwort(e): Lateral reticular nucleus ; Reticulocerebellar tract ; Spinoreticular tract ; Cerebellum ; Flexor reflex afferents
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary Mass discharges were recorded from the dissected left restiform body in unanaesthetized, decerebrate, and decerebellate cats. The spinal cord was severed in the thoracic or cervical region sparing only the left ventral quadrant. In this preparation the discharges were shown to relate largely or exclusively to activity in the reticulocerebellar tract originating from the lateral reticular nucleus. The ascending spinal tract was identified with the bilateral ventral flexor reflex tract (bVFRT) of Lundberg and Oscarsson (1962). The reticulocerebellar tract was activated from the flexor reflex afferents and nerve volleys from each of the four limbs were equally effective. It is concluded that the lateral reticular nucleus is not responsible for the somatotopically organized projection of cutaneous afferents, as assumed before. The bVFRT is strongly influenced from the cerebellar cortex and the organization of the closed loop formed between the cortex and the spinal cord is discussed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Experimental brain research 1 (1966), S. 320-328 
    ISSN: 1432-1106
    Schlagwort(e): Lateral reticular nucleus ; Reticulocerebellar tract ; Spinoreticular tract ; Cerebellum ; Flexor reflex afferents
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The experiments were done on unanaesthetized, decerebrate, and decerebellate cats. Recording was made from axons originating in the lateral reticular nucleus on stimulation of various nerves, cutaneous receptors, and certain descending tracts. Excitatory and inhibitory effects were evoked from the flexor reflex afferents of receptive fields which included most of the body surface. It is concluded that the lateral reticular nucleus with respect to its afferent inflow is similar to the non-cerebellar nuclei of the reticular formation. The possibility that the reticulocerebellar tract is important in determining the background excitation of cortical neurones is discussed. The effects evoked by stimulation of descending tracts were consistent with the disclosure that the bilateral ventral flexor reflex tract is the afferent path to the lateral reticular nucleus.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Experimental brain research 1 (1966), S. 329-337 
    ISSN: 1432-1106
    Schlagwort(e): Inferior olive ; Olivocerebellar tract ; Spinoolivary tract ; Cerebellum ; Flexor reflex afferents
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The discharges were recorded from the dissected right restiform body in unanaesthetized, decerebrate, and decerebellate cats. The spinal cord was severed in the thoracic and/or cervical region sparing only the left ventral quadrant. The discharges were shown to relate largely or exclusively to activity in the olivocerebellar tract. The olivocerebellar discharges were elicited by stimulation of the flexor reflex afferents. Large responses were evoked from the right hindlimb nerves and small responses from the left hindlimb nerves. The responses had a latency of about 20 msec. The spinoolivary tract is tentatively identified with the contralateral ventral flexor reflex tract of Lundberg and Oscarsson (1962).
    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. 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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  • 5
    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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  • 6
    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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  • 7
    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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