Modification of the Spectrophotometric Method
of the Determination of Monoamine Oxidase

Turski, W.; Turska, Ewa; Gross-Bellard, M.

doi:10.1159/000459482

Cited by 36 publications

(16 citation statements)

References 5 publications

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“…Mitochondria were prepared from the postnuclear super natant (600 g, 10 min) and purified by multiple washings in medium A (10,000 g, 10 min, 2 X 6,000 g, 10 min). Purity of the obtained mitochondrial fraction was controlled by the determination of the activity of succinate dehydrogenase (EC 1.3.99.1) [21], monoaminooxidase (EC 1.4.3.4) [24], glucose-6-phosphatase (EC 3.1.3.9) [22], acid phosphatase (EC 3.1.3.2) [2] and 5'-nucleotidase (EC 3.1.3.5) [20].…”

Section: Methodsmentioning

confidence: 99%

Studies on the Latency of Rat Liver Fumarate Hydratase1

Szkudlarek¹,

Turski²

1975

Enzyme

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A hypotonic medium and nonionic detergents Triton X-100 and digitonin have no influence on the activity of fumarase in the homogenate or in the mitochondrial fraction either. Ionic detergents of deoxycholate, cholate and sodium dodecyl sulphate exert an inhibiting influence. The activity of enzyme was determined in an L-malate-fumarate system. 1 h of incubation and the original Racker’s method gave similar results. The lack of ‘latency’, found for the mitochondrial fumarase, was discussed basing on the data concerned with the penetration of metabolites through the inner mitochondrial membrane.

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Section: Methodsmentioning

confidence: 99%

Studies on the Latency of Rat Liver Fumarate Hydratase1

Szkudlarek¹,

Turski²

1975

Enzyme

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“…The effect of the extracts on MAO activity was measured according to a previously reported method [17], with slight modification. In brief, the mixture contained 0.025 M phosphate buffer (pH 7.0), 0.0125 M semicarbazide, 10 mM benzylamine and 75 μL of MAO solu tion (EC 1.4.3.4) and 0-100 μL of the extracts.…”

Section: Mao Inhibitory Assaymentioning

confidence: 99%

In vitro neuroprotective properties of some commonly consumed green leafy vegetables in Southern Nigeria

et al. 2016

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Green leafy vegetable is one of the major cuisines in Southern Nigeria and they are not only consumed for their palatability, but also for their nutritional and medicinal properties as reported in folklore. Notable among them are afang (Gnetum africanum), editan (Lasianthera africana) and utazi (Gongronema latifolium). In this study, we investigated the effect of aqueous extracts from afang, editan and utazi leaves on cholinesterases [acetylcho linesterase (AChE) and butyrylcholinesterase (BChE)] and monoamine oxidase (MAO) activities. Fe 2+ chelating abilities were also determined as an assessment of their neuroprotective potentials in vitro. We also assayed for their total phenol contents while the constituent phenolics were characterized using high performance liquid chromatography coupled with diode array detector (HPLC-DAD). The results revealed that the extracts inhibited AChE, BChE and MAO activities and also chelated Fe 2+ in concentration dependent manner. The HPLC-DAD char acterization showed that gallic, caffeic and ellagic acids and rutin were the dominant phenolic compounds in the extracts; nevertheless, utazi had the highest distribution of identified phenolics while afang had the least. The ability of the aqueous extracts of the vegetables to inhibit key enzymes (AChE, BChE and MAO) relevant to neu rodegeneration, as well chelate metal ion could help suggest their possible neuroprotective properties. These vegetables could be use as dietary intervention in the management of neurodegenerative diseases such as Alzheimer's and Parkinson's diseases.

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“…The protein concentration was determined by using a method of [13], the assay of MAO and activity measurement of MAO with different concentrations (100-500 lg/ ml) of C. martinii was performed as per the methods [14,15] with slight modification. In brief the reaction mixture contained 0.025 M phosphate buffer of pH 7, 0.0125 M semicarbazide, 10 mM benzylamine (pH adjusted to 7), and 0.67 mg of enzyme and ethanol extract of C. martinii (100-500 lg/ml) in a total reaction volume of 2 ml.…”

Section: Determination Of Protein Assay and Activity Measurements Ofmentioning

confidence: 99%

Kinetics of Inhibition of Monoamine Oxidase Using Cymbopogon martinii (Roxb.) Wats.: A Potential Antidepressant Herbal Ingredient with Antioxidant Activity

et al. 2011

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The study was designed to evaluate the antioxidant activity and effect of Cymbopogon martinii (Roxb.) Wats. (Poaceae) leaves on the activity of monoamine oxidase and kinetics of enzyme inhibition. Ethanol extract of C. martinii and rat brain mitochondrial monoamine oxidase preparation ware used to study the kinetics of enzyme inhibition using double reciprocal LineweaverBurk plot. The DPPH was used as a source of free radical to evaluate antioxidant potential. It is observed that, the ethanolic extract of C. martinii inhibits the monoamine oxidase activity with competitive mode of inhibition. The V max (0.01 mM/min) remained constant while, K m varied from 21.00 ± 1.1, 43.33 ± 1.5 and 83.33 ± 1.4 mM for 100-500 lg/ml concentration of C. martinii. The K i values were calculated to be 90.00 ± 0.87, 75.00 ± 0.69, 68.18 ± 0.68 lg for 100-500 lg/ml concentration of C. martini. It also shows a significant DPPH (1,1-diphenyl-2-picryl hydrazine) radical scavenging (IC 50 = 0.34 ± 0.05 mg/ml) and reducing activity (IC 50 = 0.70 ± 0.22 mg/ml). The C. martini can be considered as a possible source of MAO inhibitor used in the treatment of depression and other neurological disorders.

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Modification of the Spectrophotometric Method of the Determination of Monoamine Oxidase

Cited by 36 publications

References 5 publications

Studies on the Latency of Rat Liver Fumarate Hydratase1

Studies on the Latency of Rat Liver Fumarate Hydratase1

In vitro neuroprotective properties of some commonly consumed green leafy vegetables in Southern Nigeria

Kinetics of Inhibition of Monoamine Oxidase Using Cymbopogon martinii (Roxb.) Wats.: A Potential Antidepressant Herbal Ingredient with Antioxidant Activity

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