Results 171 to 180 of about 2,006 (201)

Stereochemical course of tyramine oxidation by semicarbazide-sensitive amine oxidase

Biochemistry, 1992
Two semicarbazide-sensitive amine oxidases (SSAO's) from bovine and porcine aortic tissue were partially purified and characterized, and the stereochemical course of amine oxidation was evaluated. The porcine and bovine SSAO's were membrane bound glycoproteins, with Km values for benzylamine of 8 and 16 microM, respectively. The reactivity of SSAO with
C H, Scaman, M M, Palcic
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CULTURE MEDIUM ENHANCES SEMICARBAZIDE-SENSITIVE AMINE OXIDASE ACTIVITY

In Vitro Cellular & Developmental Biology - Animal, 2002
Components of fetal calf serum (FCS) are known to contribute to growth and maintenance of cultured cells. Fetal calf serum supplementation of media also may contribute to the cytotoxicity of other substances to cells grown in vitro. Semicarbazide-sensitive amine oxidase (SSAO) enzyme, present in FCS, metabolizes primary amines and contributes to amine ...
M B, Trent, D J, Conklin, P J, Boor
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Hypoxia inhibits semicarbazide-sensitive amine oxidase activity in adipocytes

Molecular and Cellular Endocrinology, 2015
Semicarbazide-sensitive amine oxidase (SSAO), an enzyme highly expressed on adipocyte plasma membranes, converts primary amines into aldehydes, ammonium and hydrogen peroxide, and is likely involved in endothelial damage during the course of diabetes and obesity.
Repessé, Xavier, Moldes, Marthe, Muscat, Adeline, Vatier, Camille, Chetrite, Gérard, Gille, Thomas, Planès, Carole, Filip, Anna, Mercier, Nathalie, Duranteau, Jacques, Fève, Bruno   +10 more
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Aminoacetone metabolism by semicarbazide-sensitive amine oxidase in rat aorta

Biochemical Pharmacology, 1995
High speed (105,000 g/60 min) membrane fractions from rat aorta homogenates metabolized the aliphatic amine aminoacetone (AA) to methylglyoxal (MG) with a Km of 19 +/- 3 microM, and Vmax of 510 +/- 169 nmol MG/hr/mg protein. This deaminating activity appears to be due to a semicarbazide-sensitive amine oxidase (SSAO), which is associated with smooth ...
G A, Lyles, J, Chalmers
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Subcellular Location of Semicarbazide‐Sensitive Amine Oxidase in Rat Aorta

European Journal of Biochemistry, 1980
With tyramine as substrate, a considerable part of the amine oxidase activity of rat aorta was inhibited by 0.1 mM semicarbazide. The residual activity was little affected by 1 mM semiicarbazide. Oxidation of 5‐hydroxytryptamine was not inhibited by 0.1 mM semicarbazide.
M, Wibo, A T, Duong, T, Godfraind
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Inhibition of bovine plasma semicarbazide‐sensitive amine oxidase by caffeine

Journal of Biochemical and Molecular Toxicology, 2011
AbstractSemicarbazide‐sensitive amine oxidase (SSAO) is a copper‐containing enzyme that catalyzes the oxidative deamination of endogenous and exogenous primary amines. SSAO exists in mammals both as a plasma‐soluble and as a membrane‐bound form, and its active site is able to come into contact with numerous xenobiotic, amine‐containing compounds.
A, Olivieri, K, Tipton
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Semicarbazide-sensitive amine oxidase. Its physiological significance

Pure and Applied Chemistry, 2001
Abstract Although the existence of plasma- and tissue-bound semicarbazide-sensitive amine oxidases (SSAOs) has been recognized earlier, the physiological relevance of the enzyme still remains uncertain. Recent data suggest that elevated serum SSAO activity might cause endothelial injury.
K. Magyar, Z. Mészáros, P. Mátyus
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Variation in semicarbazide-sensitive amine oxidase activity in plasma and tissues of mammals

Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology, 2000
Semicarbazide-sensitive amine oxidase (SSAO) (E.C. 1.4.3.6) is a group of enzymes with as yet poorly understood function which is widely present in nature. The variation in methodology for determination of activity, differences in substrates used and in nomenclature have made it difficult to compare SSAO in different species and tissues.
Boomsma, Frans, van Dijk, J (Jan), Bhaggoe, V, Houwen, Angelique, van den Meiracker, Ton   +4 more
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Monoamine oxidase and semicarbazide sensitive amine oxidase activities in toad liver mitochondria

Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1988
1. The deamination of 5-HT and PEA has been assayed by a radiochemical method in mitochondria isolated from toad liver. 2. Time courses of 5-HT and PEA deamination indicate that when PEA is used as the substrate, higher specific activities are obtained. 3. 5-HT is deaminated by MAO A and partially by a SSAO-like enzyme. 4. PEA is deaminated exclusively
O, Senatori, A, Nicotra
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Silicon-mediated inactivation of semicarbazide-sensitive amine oxidase

Bioorganic & Medicinal Chemistry Letters, 1995
Abstract Several organosilicon amines were synthesized as potential mechanism-based inhibitors of semicarbazide-sensitive amine oxidase (SSAO) prepared from rat aorta. 2-[Dimethyl(2-phenylethyl)silyl]-methanamine, hydrochloride produced potent time-dependent inhibition of SSAO.
Charles Danzin, Jean-Noël Collard, Pierrette Marchal, Daniel Schirlin   +3 more
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