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  • Analytical Chemistry and Spectroscopy  (1)
  • Bulimia  (1)
  • Dipeptidyl ¶peptidase IV  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European archives of psychiatry and clinical neuroscience 250 (2000), S. 86-92 
    ISSN: 1433-8491
    Keywords: Key words Anorexia ; Bulimia ; Peptidases ; Dipeptidyl ¶peptidase IV ; Neuropeptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The aim of this study was to examine whether anorexia nervosa and bulimia nervosa are accompanied by lower serum activity of dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5), a membrane-bound serine protease that catalyses the cleavage of dipeptides from the amino-terminus of oligo- and polypeptides. Substrates of DPP IV are, amongst others, neuroactive eptides, such as substance P, growth hormone releasing hormone, neuropeptide Y, and peptide YY. DPP IV activity was measured in the serum of 21 women with anorexia nervosa, 21 women with bulimia nervosa and 18 normal women. Serum ¶DPP IV activity was significantly lower in patients with anorexia nervosa and bulimia nervosa than in the normal controls. In the total study group, there were significant and inverse relationships between serum DPP IV activity and the total scores on the Bulimic Investigatory Test, Edinburgh, the Eating Disorder Inventory (EDI) and the Hamilton Depression Rating Scale. In the total study group no significant correlations between DPP IV and age, body weight or body mass index could be found. It is concluded that lowered serum DPP IV activity takes part in the pathophysiology of anorexia and bulimia nervosa. It is hypothesised that a combined dysregulation of DPP IV and neuroactive peptides, which are substrates of DPP IV, e.g. neuropeptide Y and peptide YY, could be an integral component of eating disorders.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Flavin-10-acetaldehyde ethyl hemi-alcoholate obtained at the Hannah Dairy Research Institute by bacterial degradation of riboflavin was examined in the Electron Attachment (EA) apparatus at the Forschungsinstitut Manfred von Ardenne. At low temperatures pyrolysis was negligible and the peak of greatest mass was only four units less than the molecular weight. The fragmentation patterns at greater field strengths indicated metastable peaks of masses in accord with the fragmentation pattern at lower fields. The patterns at the lower temperatures used resembled in important respects the EA pattern from riboflavin in an earlier study. In explanation of the fragmentation pattern obtained, structures have been assigned to the ions recorded.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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