[54] Amine oxidases

Tabor, Celia White; Tabor, Herbert; Rosenthal, Sanford M.

doi:10.1016/s0076-6879(55)02218-0

Cited by 136 publications

(121 citation statements)

References 4 publications

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“…Development was done with gradient elution of 2.5 N HCl under essentially the same conditions described by Tabor et af. 5) Another reaction product, 1,3-diaminopropane, was measured colorimetrically with ninhydrin after the column was developed.…”

Section: Methodsmentioning

confidence: 99%

Characterization of Membrane-bound Spermidine Dehydrogenase ofCitrobacter freundii

Hisano

Murata

Kimura

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

Characterization of Membrane-bound Spermidine Dehydrogenase ofCitrobacter freundii

Hisano

Murata

Kimura

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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“…Beef plasma amine oxidase was purified as in [3] . Enzyme activity was assayed spectrophotometrically as in [4]. Enzyme kinetics were studied by poiarographic determination of oxygen uptake in a GME oxygraph model KM, equipped with a Clark electrode, in a 1.5 ml reaction vessel, thermostated at 38'C with 0.1 M potassium phosphate buffer, pH 8, Enzyme units are expressed according to [S] .…”

Section: Methodsmentioning

confidence: 99%

Inhibition of beef plasma amine oxidase activity by glycine

et al. 1978

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“…4). [20][21][22] DISCUSSION Several types of amine oxidases catalyze the oxidative deamination of various endogenous and xenobiotic amines in mammalian tissues. By now, determination of the substrate selectivity of amine oxidases has been based on the sensitiv- A respective cDNA of rat amine oxidases were transfected into COS-1 cells.…”

Section: Influence Of Amine Oxidase Inhibitorsmentioning

confidence: 99%

“…In contrast, semicarbazide has a weak inhibitory effect on MAO at a concentration of 0.1-1 mM. 10) Clorgyline and deprenyl have been regarded as virtually inactive against the tissue-bound SSAO, nevertheless they showed moderate reversible competitive inhibition against bovine 11) and human 12,13) plasma SSAO at a concentration of 0.1-1 mM. DAO, belonging to the Cu-AOs, is responsible for histamine metabolism.…”

mentioning

confidence: 99%

Substrate Selectivity of Monoamine Oxidase A, Monoamine Oxidase B, Diamine Oxidase, and Semicarbazide-Sensitive Amine Oxidase in COS-1 Expression Systems

Ochiai

Itoh

Sakurai³

et al. 2006

Biological & Pharmaceutical Bulletin

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Amine oxidases (AOs) are widely distributed among all living organisms. 1) This class of enzymes is divided into two subclasses: FAD-containing amine oxidases (FAD-AOs) and Cu-containing amine oxidases (Cu-AOs). Two types of mitochondrial monoamine oxidases, monoamine oxidases (MAO)-A and MAO-B, and cytosolic polyamine oxidase are included in FAD-AOs.2) The Cu-AOs consist of retina amine oxidase, diamine oxidase (DAO), and semicarbazide-sensitive amine oxidase (SSAO), which is known as the tissue-bound or plasma form of amine oxidase. The classification of MAO into an A and B form was primarily based on Johnston's presentation that both enzymes could be differentiated with the aid of the specific inhibition of MAO-A by clorgyline and of MAO-B by deprenyl. 3) Classification by means of specific inhibitors has been more convenient for the identification of different types of amine oxidase. However, this concept has been considered somewhat of an oversimplification and the premises on which it was based have come under increasing scrutiny. [4][5][6][7][8][9] One major problem was that serotonin and b-phenylethylamine, which are generally used to distinguish MAO-A and MAO-B, are not entirely specific for the respective MAO form. Another problem was that the substrate selectivity of MAO seems to be affected by minor cross-inhibition caused by specific inhibitors.SSAO essentially metabolizes amine compounds as well as MAO-A and MAO-B. However, the enzyme activity is not inhibited by clorgyline and deprenyl, whereas it is almost completely inhibited by semicarbazide. In contrast, semicarbazide has a weak inhibitory effect on MAO at a concentration of 0.1-1 mM. 10) Clorgyline and deprenyl have been regarded as virtually inactive against the tissue-bound SSAO, nevertheless they showed moderate reversible competitive inhibition against bovine 11) and human 12,13) plasma SSAO at a concentration of 0.1-1 mM. DAO, belonging to the Cu-AOs, is responsible for histamine metabolism. 14) Comparative substrate selectivity studies of DAO have not always been performed in detail. Aminoguanidine has been used for many years as an inhibitor of Cu-AO, but it is a relatively weak and nonselective inhibitor of SSAO. 15) Thus, the results of the substrate selectivity of these amine oxidases using specific inhibitors are very confused and complex, and might not reflect natural biochemical properties. In this study, we utilized a single amine oxidase expressed in COS-1 cells to investigate the substrate selectivity of amine oxidases in the absence of chemical inhibitors. MATERIALS AND METHODSAnimals Nine-week-old male Wistar rats purchased from Japan SLC (200-220 g, Hamamatsu, Japan) were housed at a constant temperature (23Ϯ1°C) and humidity (55Ϯ5%) with automatically controlled lighting (07:00-19:00).Plasmid Construction Standard protocols were used for all recombinant DNA technology. 16) The full-length ORF AOs plasmid was constructed as follows. Total RNA was isolated using the Wizard SV Total RNA Extraction Kit (Promega, Madison, WI,...

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[54] Amine oxidases

Cited by 136 publications

References 4 publications

Characterization of Membrane-bound Spermidine Dehydrogenase ofCitrobacter freundii

Characterization of Membrane-bound Spermidine Dehydrogenase ofCitrobacter freundii

Inhibition of beef plasma amine oxidase activity by glycine

Substrate Selectivity of Monoamine Oxidase A, Monoamine Oxidase B, Diamine Oxidase, and Semicarbazide-Sensitive Amine Oxidase in COS-1 Expression Systems

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