Results 131 to 140 of about 1,805,611 (181)
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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Semicarbazide-sensitive amine oxidase in transgenic mice with diabetes
Biochemical and Biophysical Research Communications, 2004 Semicarbazide-sensitive amine oxidase (SSAO) activity in plasma is increased in diabetes, and in particular, in diabetic patients with vascular complications. It has been speculated that SSAO is involved in the development of such complications due to the production of cytotoxic compounds.
C, Gokturk +5 more
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Methylamine metabolism to formaldehyde by vascular semicarbazide-sensitive amine oxidase
Toxicology, 1992The capacity of the vascular enzyme, semicarbazide-sensitive amine oxidase (SSAO), to metabolize methylamine to the potentially toxic product, formaldehyde, was tested using rat aortic homogenates and purified porcine aortic SSAO. Formaldehyde production in incubations of enzyme source with methylamine (1 mM) was detected by high performance liquid ...
G A S Ansari +2 more
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Developmental Vasculotoxicity Associated with Inhibition of Semicarbazide-Sensitive Amine Oxidase
Toxicology and Applied Pharmacology, 1999The endogenous substrate(s) and physiological function(s) of semicarbazide-sensitive amine oxidase (SSAO), a group of enzymes exhibiting highest activity in vascular smooth muscle cells of the mammalian aortic wall, remain undetermined. This study examines the pathophysiological effects in the thoracic aortic wall resulting from specific in vivo SSAO ...
P J Boor, Paul J Boor, M B Trent
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Diabetes and semicarbazide-sensitive amine oxidase (SSAO) activity: A review
Life Sciences, 2006The enzyme of semicarbazide-sensitive amine oxidase (SSAO) activity has been reported to be elevated in blood from diabetic patients. SSAO are widely distributed in plasma membranes of various tissues and blood plasma. SSAO-mediated production of toxic aldehydes has been proposed to be related to pathophysiological conditions.
Toshio Obata
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Stability of semicarbazide-sensitive amine oxidase in human blood and plasma
Clinica Chimica Acta, 1998Frans Boomsma
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The inhibition of semicarbazide-sensitive amine oxidase by aminohexoses
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003Semicarbazide-sensitive amine oxidase (EC 1.4.3.6; amine:oxygen oxidoreductase (deaminating) (copper-containing); SSAO) is a multifunctional protein. It acts under inflammatory conditions as a vascular-adhesion protein (VAP-1), mediating the adhesion of lymphocytes to vascular endothelial cells. The relationships, if any, between this adhesion function
Jeffrey, O'Sullivan +5 more
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Plasma Semicarbazide-Sensitive Amine Oxidase in Stroke
European Neurology, 1999Semicarbazide-sensitive amine oxidase (SSAO) has been suggested to be involved in the development of vascular endothelial damage. The source of the soluble form of SSAO found in the blood serum is unknown. However, it has been speculated that it is secreted from cells within the vascular wall where high activity of the enzyme is found.
H, Garpenstrand +4 more
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Semicarbazide-Sensitive Amine Oxidase: Current Status and Perspectives
Current Medicinal Chemistry, 2004Semicarbazide-sensitive amine-oxidase (SSAO) is present in various human tissues and in plasma. Oxidative deamination of short-chain aliphatic amines is catalyzed by this enzyme to afford the corresponding aldehydes, ammonia and hydrogen peroxide. Methylamine and aminoacetone have been recognized to be physiological substrates for SSAO.
P. Mátyus +5 more
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Some properties of semicarbazide-sensitive amine oxidases
1987The 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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