Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Distribution and properties of human intestinal diamine oxidase and its relevance for the histamine catabolism
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 756 (1983), S. 196-203 
    Details
    ISSN: 0304-4165
    Keywords: (Human intestine) ; Diamine oxidase ; Histamine catabolism
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0304-4165(83)90092-2
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Human intestinal diamine oxidase: Substrate specificity and comparative inhibitor study (1980)
    Springer
    Inflammation research 10 (1980), S. 108-110 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract For an 80-fold purified preparation of human intestinal diamine oxidase the optimum conditions of incubation, the substrate and the inhibitor specificity were tested. Putrescine was the most favoured substrate butN τ-methylhistamine and 2-methylhistamine were metabolized at optimum conditions with nearly the same velocity. Histamine reached about 50% of the reaction velocity of putrescine. Aminoguanidine and semicarbazide inhibited the human intestinal enzyme like a classical diamine oxidase. However, a distinct inhibition of human intestinal and pea seedling diamine oxidase was observed in presence of β-aminopropionitrile (weak inhibition of the human enzyme, strong inhibition of pea seedling diamine oxidase) and burimamide (strong inhibition of human intestinal enzyme, nearly no influence on pea seedling diamine oxidase). It is proposed to differentiate on the basis of functional considerations diamine oxidases with more histamine detoxicating activities from those being more involved in regulating polyamine levels in growing tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02024190
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    The start of a programme for measuring diamine oxidase activity in biopsy specimens of human rectal mucosa (1981)
    Springer
    Inflammation research 11 (1981), S. 33-37 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In human subjects, apart from in the kidney, diamine oxidase occurs mainly in the gut. Therefore this enzyme can be used as an indicator of intestinal integrity. In biopsies of rectal mucosa the diamine oxidase activity was assayed in 55 patients, 41 having a histologically normal mucosa and 14 being diseased. The determinations of the enzymic activity were supervised by statistical quality control. In the unchanged rectal mucosa the diamine oxidase activity was 40 nmol/min×g on average. In 7 patients with rectal polyps the enzymic activity was significantly diminished in these benign tumours (x=7.7 nmol/min×g) apart from one, where it was elevated. A decrease in diamine oxidase activity was further observed in rectal carcinoma and ulcerative colitis. Whether the reduction of intestinal diamine oxidase activity accompanies premalignant or malignant states or whether it is a general sign of a disturbance of intestinal integrity remains questionable.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01991451
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Intestinal monoamine oxidase: Does it have a role in histamine catabolism? (1982)
    Springer
    Inflammation research 12 (1982), S. 53-59 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The importance of intestinal diamine oxidase in histamine catabolism was proved in several series of experiments. However, intestinal monoamine oxidase might also be involved in histamine degradation either by direct deamination or by the deamination of methylated products. The soluble fraction of intestinal monoamine oxidase was purified and tested for its properties and substrate specificity by three different methods which are described in detail. Using 0.15M phosphate buffer the optimum pH was 7.4–7.6. TheK m values for serotonin and tyramine were 0.2 and 0.3×10−3 M. The most favoured substrates of the enzyme were tyramine, tryptamine and serotonin, but it was not pissible to classify the enzyme as a type A or B monoamine oxidase only by its substrate specificity. Histamine and ring methylated derivatives were not attacked by intestinal monoamine oxidase. This means that in the intestinal mucosa the oxidative pathway of histamine is completely catalysed by diamine oxidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01965107
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    The influence of carcinoma growth on diamine oxidase activity in human gastrointestinal tract (1980)
    Springer
    Inflammation research 10 (1980), S. 110-113 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The distribution of diamine oxidase (DAO) activity was studied in patients having no carcinoma disease. Besides in gut DAO occurred in high activity only in kidney and mesenteric lymph nodes. In patients with adenocarcinoma of the large bowel or of the stomach the enzymic activity was reduced in the tumour tissue itself as compared with the adjacent mucosa in which part the highest activities were observed. In stomach it seemed most important that the enzymic activity was enhanced in the whole mucosa, also in a 10 cm distance from tumour where no histological alterations were found. This fact should be checked for significance in early tumour diagnosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02024191
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...