Radiochemical Assay of Monoamine Oxidase Activity.
5-Hydroxytryptamine
Benzylamine
Discontinuous assay
Liquid scintillation counting
Monoamine oxidase
Organic extraction
Radiolabeled amine
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
28
9
2022
pubmed:
29
9
2022
medline:
1
10
2022
Statut:
ppublish
Résumé
The activity of monoamine oxidase enzymes may be quantified by measuring the conversion of a radiolabeled amine substrate to a radiolabeled product that occurs during incubation of the substrate with the enzyme in an aqueous buffer. Described herein is an established discontinuous procedure in which separation of the substrate and product is achieved by extracting uncharged aldehydes into an organic solvent, while cationic amines remain in an acidified aqueous layer. Under assay conditions designed to ensure a pseudo-linear catalytic rate for the duration of the incubation, determination of radioactivity in the organic solvent by liquid scintillation counting facilitates estimation of an initial rate for amine turnover.
Identifiants
pubmed: 36169855
doi: 10.1007/978-1-0716-2643-6_5
doi:
Substances chimiques
Aldehydes
0
Amines
0
Radiopharmaceuticals
0
Solvents
0
Monoamine Oxidase
EC 1.4.3.4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
45-61Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Zhou M, Panchuk-Voloshina N (1997) A one-step fluorometric method for the continuous measurement of monoamine oxidase activity. Anal Biochem 237:169–174
doi: 10.1006/abio.1997.2392
Nelson DR, Huggins AK (1974) Interference of 5-hydroxytryptamine in the assay of glucose by glucose oxidase:peroxidase:chromogen based methods. Anal Biochem 59:46–53
doi: 10.1016/0003-2697(74)90007-4
Holt A, Palcic MM (2006) A peroxidase-coupled continuous absorbance plate-reader assay for flavin monoamine oxidases, copper-containing amine oxidases and related enzymes. Nat Protoc 1(5):2498–2505
doi: 10.1038/nprot.2006.402
Carpene C, Les F, Mercader J, Gomez-Zorita S, Grolleau JL, Boulet N, Fontaine J, Iglesias-Osma MC, Garcia-Barrado MJ (2020) Opipramol inhibits lipolysis in human adipocytes without altering glucose uptake and differently from antipsychotic and antidepressant drugs with adverse effects on body weight control. Pharmaceuticals (Basel) 13(3). https://doi.org/10.3390/ph13030041
Wurtman RJ, Axelrod J (1963) A sensitive and specific assay for the estimation of monoamine oxidase. Biochem Pharmacol 12:1439–1441. https://doi.org/10.1016/0006-2952(63)90215-6
doi: 10.1016/0006-2952(63)90215-6
pubmed: 14096433
Jain M, Sands F, Von Korff RW (1973) Monoamine oxidase activity measurements using radioactive substrates. Anal Biochem 52(2):542–554. https://doi.org/10.1016/0003-2697(73)90060-2
doi: 10.1016/0003-2697(73)90060-2
pubmed: 4698849
Tipton KF, Youdim MB (1976) Assay of monoamine oxidase. Ciba Symposium 39:393–403
Tipton KF, Youdim MBH (1983) The assay of monoamine oxidase activity. In: Parvez S, Nagatsu T, Nagatsu I, Parvez H (eds) Methods in biogenic amine research. Elsevier Science Publishers B.V., pp 441–465
Lyles GA, Callingham BA (1982) In vitro and in vivo inhibition by benserazide of clorgyline-resistant amine oxidases in rat cardiovascular tissues. Biochem Pharmacol 31(7):1417–1424
doi: 10.1016/0006-2952(82)90037-5
Pisano JJ (1960) A simple analysis for normetanephrine and metanephrine in urine. Clin Chim Acta 5:406–414. https://doi.org/10.1016/0009-8981(60)90146-7
doi: 10.1016/0009-8981(60)90146-7
pubmed: 14433251
Holt A, Baker GB (1996) Inhibition of rat brain monoamine oxidase enzymes by fluoxetine and norfluoxetine. Naunyn-Schmedeberg’s Arch Pharmacol 354:17–24
Ramsay RR, Olivieri A, Holt A (2011) An improved approach to steady-state analysis of monoamine oxidases. J Neural Transm 118(7):1003–1019. https://doi.org/10.1007/s00702-011-0657-y
doi: 10.1007/s00702-011-0657-y
pubmed: 21643793
Hall DW, Logan BW, Parsons GH (1969) Further studies on the inhibition of monoamine oxidase by M and B 9302 (clorgyline). I. Substrate specificity in various mammalian species. Biochem Pharmacol 18(6):1447–1454
doi: 10.1016/0006-2952(69)90258-5
Fowler CJ, Mantle TJ, Tipton KF (1982) The nature of the inhibition of rat liver monoamine oxidase types A and B by the acetylenic inhibitors clorgyline, l-deprenyl and pargyline. Biochem Pharmacol 31(22):3555–3561
doi: 10.1016/0006-2952(82)90575-5
Fuentes JA, Neff NH (1977) Inhibition of pargyline of cardiovascular amine oxidase activity. Biochem Pharmacol 26:2107–2112
doi: 10.1016/0006-2952(77)90259-3
Lyles GA, Callingham BA (1975) Evidence for a clorgyline-resistant monoamine metabolizing activity in the rat heart. J Pharm Pharmacol 27:682–691
doi: 10.1111/j.2042-7158.1975.tb09532.x
Clarke DE, Lyles GA, Callingham BA (1982) A comparison of cardiac and vascular clorgyline-resistant amine oxidase and monoamine oxidase. Inhibition by amphetamine, mexiletine and other drugs. Biochem Pharmacol 31(1):27–35
doi: 10.1016/0006-2952(82)90231-3
Jones TZ, Balsa D, Unzeta M, Ramsay RR (2007) Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better. J Neural Transm 114(6):707–712. https://doi.org/10.1007/s00702-007-0675-y
doi: 10.1007/s00702-007-0675-y
pubmed: 17401535
Wang J, Edmondson DE (2011) (2)H kinetic isotope effects and pH dependence of catalysis as mechanistic probes of rat monoamine oxidase A: comparisons with the human enzyme. Biochemistry 50(35):7710–7717. https://doi.org/10.1021/bi200951z
doi: 10.1021/bi200951z
pubmed: 21819071
Kinemuchi H, Arai Y, Oreland L, Tipton KF, Fowler CJ (1982) Time-dependent inhibition of monoamine oxidase by ß-phenethylamine. Biochem Pharmacol 31(6):959–964
doi: 10.1016/0006-2952(82)90327-6
Holt A, Sharman D, Callingham BA (1992) Effects in-vitro of procarbazine metabolites on some amine oxidase activities in the rat. J Pharm Pharmacol 44:494–499
doi: 10.1111/j.2042-7158.1992.tb03653.x
May ME (1980) A caution in the use of tritiated substrates for monoamine oxidase assays. J Neurochem 35(6):1453–1454. https://doi.org/10.1111/j.1471-4159.1980.tb09023.x
doi: 10.1111/j.1471-4159.1980.tb09023.x
pubmed: 7003064
McDonald GR, Hudson AL, Dunn SM, You H, Baker GB, Whittal R, Martin JW, Jha A, Edmondson DE, Holt A (2008) Bioactive contaminants leach from disposable laboratory plasticware. Science 322:917
doi: 10.1126/science.1162395
Olivieri A, Degenhardt OS, McDonald GR, Narang D, Paulsen IM, Kozuska JL, Holt A (2012) On the disruption of biochemical and biological assays by chemicals leaching from disposable laboratory plasticware. Can J Physiol Pharmacol 90(6):697–703. https://doi.org/10.1139/y2012-049
doi: 10.1139/y2012-049
pubmed: 22509735
Otsuka S, Kobayashi Y (1964) Radioisotopic assay for monoamine oxidase determinations in human plasma. Biochem Pharmacol 13:995–1006. https://doi.org/10.1016/0006-2952(64)90096-6
doi: 10.1016/0006-2952(64)90096-6
pubmed: 14201142
Wang J, Edmondson DE (2010) High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: comparison with human MAO A. Protein Expr Purif 70(2):211–217. https://doi.org/10.1016/j.pep.2009.10.013
doi: 10.1016/j.pep.2009.10.013
pubmed: 19883764
Ramsay RR (1991) Kinetic mechanism of monoamine oxidase A. Biochemistry 30(18):4624–4629
doi: 10.1021/bi00232a038
Newton-Vinson P, Hubalek F, Edmondson DE (2000) High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif 20(2):334–345. https://doi.org/10.1006/prep.2000.1309 . S1046-5928(00)91309-3 [pii]
doi: 10.1006/prep.2000.1309
pubmed: 11049757
Upadhyay AK, Edmondson DE (2008) Characterization of detergent purified recombinant rat liver monoamine oxidase B expressed in Pichia pastoris. Protein Expr Purif 59(2):349–356. https://doi.org/10.1016/j.pep.2008.03.002
doi: 10.1016/j.pep.2008.03.002
pubmed: 18424170
pmcid: 2445446
Kessler MJ (1989) Statistics of liquid scintillation counting. In: Kessler MJ (ed) Liquid scintillation analysis: Science and technology. Packard Instrument Company, Waltham, MA
Cook PF, Cleland WW (2007) Enzyme kinetics and mechanism. Taylor & Francis Group, New York
doi: 10.4324/9780203833575