Results 161 to 170 of about 21,283 (210)
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Inhibition of diamine oxidases and polyamine oxidases by diamine-based compounds

Journal of Neural Transmission, 2007
This review reports on inhibitors of copper-containing amine oxidases and flavoprotein polyamine oxidases, which are structurally based on diamines. In the introduction, basic characteristics and classification of amine oxidases are described together with the significance of their synthetic inhibitors.
M, Sebela, M, Tylichová, P, Pec
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Serum Diamine Oxidase in the Neonate

Neonatology, 1986
Serum diamine oxidase (DAO) activities were measured in 9 pregnant women and in 33 neonates during the 1st week of life. The radiometric method was used. Very high values were found in the mothers (mean ± SE: 720 ± 143 pmol ml<sup>-1</sup> h<sup>-1</sup>) Neonates showed significantly elevated values (mean ± SE: 178 ± 54 pmol ml&
FORGET P, DE CURTIS, MARIO, SENTERRE J.
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Differentiation of monoamine oxidase and diamine oxidase

Biochemical Pharmacology, 1962
Abstract In kidney of cats pretreated with inhibitors of monoamine oxidase and diamine oxidase the activity of these enzymes was measured simultaneously, using typical cell fractions and substrates. After iproniazid pretreatment inhibition of diamine oxidase occurred somewhat earlier and was of shorter duration than inhibition of monoamine oxidase ...
W P, BURKARD, K F, GEY, A, PLETSCHER
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Inhibition of diamine oxidase by bulbocapnine

Biochemical Pharmacology, 1962
Abstract Using a modification of the spectrophotofluorometric method of Shore, Burkhalter and Cohn, an inhibition of diamine oxidase by bulbocapnine, using histamine as a substrate, has been demonstrated. The mechanism of the inhibition is competitive, as indicated by Lineweaver-Burke and Hunter-Downs plots.
J E, CHAPMAN, E J, WALASZEK
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Quantification of human diamine oxidase

Clinical Biochemistry, 2017
Diamine oxidase (DAO) is essential for extracellular degradation of histamine. For decades activity assays with inherent limitations were used to quantify the relative amounts of DAO. No reference DAO standard is available. Absolute DAO amounts cannot be determined. Controversy exists, whether DAO is circulating or not in non-pregnant individuals.
Thomas Boehm   +9 more
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Subcellular distribution of diamine oxidase

Comparative and General Pharmacology, 1970
1. 1. Subcellular distribution of diamine oxidase (DAO) was studied in various mammalian tissues using differential centrifugation. 2. 2. Highest DAO activity was found in the 600 g pellets (nuclear fraction) of the following tissues: kidney cortex (cat and dog), cat intestine, rabbit placenta, and rat uterus with deciduomata. 3. 3.
B, Backus, K S, Kim
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The oxidation of cystamine and other sulfur-diamines by diamine-oxidase preparations

Experientia, 1956
Le diamine solforate cistamina e lantionamina sono ossidate con velocita comparabile a quella della cadaverina dalla diamino-ossidasi. Il solfone della lantionamina e ossidato piu lentamente ed il disolfossido della cistamina non e ossidato affatto.
D, CAVALLINI, C, DE MARCO, B, MONDOVI
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Diamine Oxidase: An Overview of Historical, Biochemical and Functional Aspects

Digestive Diseases, 1994
This 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, 1969
Abstract 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, 1980
The 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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