Literature DB >> 4075526

Assay of platelet monoamine oxidase in whole blood.

G M van Kempen, J L van Brussel, E J Pennings.   

Abstract

Monoamine oxidase (MAO; EC 1.4.3.4.) was measured in whole blood with kynuramine as the substrate. Optimal circumstances were determined. By use of selective inhibitors, gradient centrifugation, dilution of samples and removal of thrombocytes from whole blood it was shown that this assay of MAO in whole blood is in fact a determination of platelet MAO. No reversible endogenous inhibitors are present in the blood. Because preparation of platelet-rich plasma may lead to considerable losses of specific subpopulations with relatively low or high enzyme activities, the advantage of using whole blood is that the MAO activity is determined in the whole platelet population.

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Year:  1985        PMID: 4075526     DOI: 10.1016/0009-8981(85)90352-3

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  2 in total

1.  Specific genetic deficiencies of the A and B isoenzymes of monoamine oxidase are characterized by distinct neurochemical and clinical phenotypes.

Authors:  J W Lenders; G Eisenhofer; N G Abeling; W Berger; D L Murphy; C H Konings; L M Wagemakers; I J Kopin; F Karoum; A H van Gennip; H G Brunner
Journal:  J Clin Invest       Date:  1996-02-15       Impact factor: 14.808

2.  X-linked borderline mental retardation with prominent behavioral disturbance: phenotype, genetic localization, and evidence for disturbed monoamine metabolism.

Authors:  H G Brunner; M R Nelen; P van Zandvoort; N G Abeling; A H van Gennip; E C Wolters; M A Kuiper; H H Ropers; B A van Oost
Journal:  Am J Hum Genet       Date:  1993-06       Impact factor: 11.025

  2 in total

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