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Diamine Oxidase: An Overview of Historical, Biochemical and Functional Aspects
Digestive Diseases, 2008This article is a review of the historical, biochemical, and functional aspects of the enzyme diamine oxidase (DAO). The amine oxidase DAO, formerly called histaminase, is found in various tissues, but is especially active in the intestinal mucosa.
Wolvekamp, M. C.J., De Bruin, R. W.F.
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Release of diamine oxidase by heparin in the rat
Biochemical Pharmacology, 1969Abstract Heparin produces a substantial rise in diamine oxidase activity in rat plasma. An increase in the plasma is evident within 10 min of an intravenous (i.v.) injection of heparin and a peak is observed between 30 and 60 min. The rise in the plasma can be accounted for by the release of diamine oxidase from the intestine, since the enzyme ...
Y, Kobayashi, J, Kupelian, D V, Maudsley
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Inhibition of diamine oxidase by antimalarial drugs
Agents and Actions, 1980The antimalarial drugs amodiaquine, quinacrine and chloroquine inhibit the catabolism of putrescine by the rat. Amodiaquine, the most potent of the three, does so in a dose-dependent fashion. This is attributed to the action in vivo of the drugs on diamine oxidase, an enzyme that is inhibited by them in vitro.
K, Ma, T L, Sourkes
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Purification of human placenta diamine oxidase
Biochemical and Biophysical Research Communications, 1992Diamine oxidase (histaminase) is produced at very high levels by the decidual cells of the placenta. The presence of diamine oxidase has been demonstrated in human neutrophils. Purification of human placenta diamine oxidase was performed by four subfractionation steps and led to the isolation of one polypeptide whose molecular weight was 84,000, as ...
F, Morel, A, Surla, P V, Vignais
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Colorimetric estimation of diamine oxidase activity
Analytical Biochemistry, 1975Abstract A simple colorimetric method for estimation of DAO activity with 4-nitrobenzylamine as a substrate (9,10) was developed. Sensitivity of this method, based on conversion of the aldehyde formed in course of the enzymatic reaction into its 4-nitrophenylhydrazone with subsequent measuring of optical density at 590 nm in strongly alkaline medium,
M I, Tourkov +4 more
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1981
The classic bioassays for progesterone and biologically active progestins are tedious and semiquantitative. These assays and their limitations were described recently (Glasser, 1975). The synthesis of RNA was suggested by Glasser (1975) to be a reasonably specific and reproducible quantitative biochemical endpoint for the action of progestins on the ...
C. H. Spilman +2 more
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The classic bioassays for progesterone and biologically active progestins are tedious and semiquantitative. These assays and their limitations were described recently (Glasser, 1975). The synthesis of RNA was suggested by Glasser (1975) to be a reasonably specific and reproducible quantitative biochemical endpoint for the action of progestins on the ...
C. H. Spilman +2 more
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Postheparin-diamine oxidase (histaminase) in anaphylaxis
Klinische Wochenschrift, 1975The level of plasma postheparin-diamine oxidase was determined in two patients three days after an anaphylactic shock and was controlled four weeks, and also six months later. A decrease of the enzyme levels to about 10% of a control group was found and a slow enzyme increase to about 40% observed six months later. It seems probable that in anaphylaxis
V, Gäng, W, Gaubitz, U, Gunzer
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Purification of human intestinal diamine oxidase
Inflammation Research, 1996Diamine oxidase (DAO; EC 1.4.3.6) catalyzes the oxidative deamination of histamine and other biogenie amines [1]. In mammals, degradation by DAO is the major pathway ofhistamine inactivation in many organs, especially in the intestine where the highest activities of DAO have been reported [2].
H G, Schwelberger, J, Sattler, E, Bodner
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Inhibition of Diamine Oxidase Activity by Metronidazole
Biochemical and Biophysical Research Communications, 1995Metronidazole was found to be a non-competitive inhibitor of man, rabbit and rat intestinal diamine oxidases with an inhibition constant value of approximately 10(-4) M. The purified bovine serum amine oxidase was not inhibited, whereas the purified swine kidney enzyme gave similar results.
O, Befani +4 more
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Immunohistochemical demonstration of lentil diamine oxidase.
Cellular and molecular biology, 1985[No abstract available]
R. Federico +3 more
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