Results 161 to 170 of about 2,006 (201)
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Some properties of semicarbazide-sensitive amine oxidases

1987
The semicarbazide-sensitive amine oxidases (SSAOs) comprise a substantial but diffuse group of enzymes separable from classical monoamine oxidase in several respects. Differences in cofactor requirement, molecular weight and subcellular distribution are crucial for such a separation.
B A, Callingham, M A, Barrand
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Semicarbazide-sensitive amine oxidases in pig dental pulp

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
The behaviour of semicarbazide-sensitive amine oxidase (SSAO; E.C. 1.4.3.6) in dental pulp has been studied, with particular reference to the metabolism of 5-hydroxytryptamine (5-HT; serotonin). Kinetic studies using radioactively labelled substrates have confirmed benzylamine, 2-phenylethylamine (PEA) and 5-HT to be substrates for microsomal SSAO from
Michael, O'Sullivan   +4 more
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Semicarbazide-sensitive amine oxidase in pig heart

1998
A semicarbazide-sensitive amine oxidase (SSAO) (E.C.1.4.3.6) has been purified from pig heart. Western blot analysis showed that the enzyme reacts with a polyclonal antibody raised against homogeneous crystalline pig plasma benzylamine oxidase (BAO). A subunit molecular mass of 97 KDa obtained by SDS electrophoresis is identical to the plasma enzyme ...
T G, Dowling, S, Cambi, F, Buffoni
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Semicarbazide-Sensitive Amine Oxidase (SSAO) in the Brain

Neurochemical Research, 2002
Semicarbazide-sensitive amine oxidase (SSAO) is widely distributed in almost tissues. However, its presence in brain microvessels is still controversial. The affinity of SSAO towards benzylamine (Bz) is considerably higher than that of monoamine oxidase (MAO). SSAO plays a role in the toxicity of several environmental and endogenous amines.
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Some aspects of the pharmacology of semicarbazide-sensitive amine oxidases

1990
Semicarbazide-sensitive amine oxidase enzymes (SSAO) are found in animals, plants, fungi and bacteria. In vertebrates, their distribution in tissues and blood plasma varies between species. Studies of the SSAO enzymes have concentrated on their biochemical identities separate from those of MAO.
B A, Callingham, A, Holt, J, Elliott
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Anti-Inflammatory Effects of Inhibiting the Amine Oxidase Activity of Semicarbazide-Sensitive Amine Oxidase

The Journal of Pharmacology and Experimental Therapeutics, 2005
Human semicarbazide-sensitive amine oxidase (SSAO) or vascular adhesion protein-1 (VAP-1) is a copper-containing amine oxidase (AOC3, EC 1.4.3.6) that has both enzymatic and adhesive function. SSAO catalyzes the oxidative deamination of primary amines, resulting in the formation of the corresponding aldehyde and release of hydrogen peroxide and ammonia.
Luisa M, Salter-Cid   +7 more
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Plasma semicarbazide-sensitive amine oxidase in human (patho)physiology

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
Semicarbazide-sensitive amine oxidases (SSAO) are widely distributed enzymes, with as yet not fully elucidated functions and roles, present in many tissues but also circulating in plasma. The enzyme also functions as an adhesion molecule, the vascular adhesion protein-1.
Boomsma, Frans   +3 more
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Semicarbazide-sensitive amine oxidase kills African trypanosomes in vitro

Acta Tropica, 2011
The African trypanosome Trypanosoma brucei is the cause of sleeping sickness in humans and Nagana in animals. Here we report that semicarbazide-sensitive amine oxidases (SSAOs), enzymes that are abound in T. brucei mammal hosts, eliminate trypanosomes by oxidation of its substrate in vitro. SSAO and its endogenous substrate methylamine are not toxic to
Qiao-Ping, Wang   +4 more
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Semicarbazide-Sensitive Amine Oxidases: Enzymes with Quite a Lot to Do

NeuroToxicology, 2004
The semicarbazide-sensitive amine oxidases (SSAO) (EC 1.4.3.6) were believed to be detoxifying enzymes, primarily involved in the oxidative deamination of endogenous amines, such as methylamine and aminoacetone, together with some xenobiotic amines. However, it appears that the reaction products may have important signalling functions in the regulation
Jeff, O'Sullivan   +5 more
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Monoamine oxidase and semicarbazide-sensitive amine oxidase activities in bovine eye

1990
The activities of MAO-A, MAO-B and the semicarbazide-sensitive amine oxidase (SSAO) were determined in bovine lens, retina, optic nerve, iris and epithelium. No activities were detected in lens but the SSAO activity was found to be rather evenly distributed in the other tissues.
A, Fernandez de Arriba   +3 more
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