Some factors influencing the metabolism of benzylamine by type A and B monoamine oxidase in rat heart and liver
Identifieur interne : 002B68 ( Main/Exploration ); précédent : 002B67; suivant : 002B69Some factors influencing the metabolism of benzylamine by type A and B monoamine oxidase in rat heart and liver
Auteurs : David Parkinson [Royaume-Uni] ; Geoffrey A. Lyles [Royaume-Uni] ; Barbara J. Browne [Royaume-Uni] ; Brian A. Callingham [Royaume-Uni]Source :
- Journal of Pharmacy and Pharmacology [ 0022-3573 ] ; 1980-09.
Abstract
The ability of MAO‐A and MAO‐B to metabolize benzylamine in vitro has been investigated in mitochondrial preparations from rat liver and heart. Although under normal circumstances benzylamine appeared to be metabolized exclusively by MAO‐B in the rat liver, a contribution by both MAO‐A and a clorgyline‐resistant enzyme component was revealed when the MAO‐B activity was much reduced by pretreatment of the mitochondria with appropriate concentrations of deprenyl. These three enzyme activities also contributed to benzylamine deamination in rat heart mitochondria. However, binding studies with [3 H]pargyline, which provided an estimate of the respective concentrations of MAO‐A and MAO‐B active centres in heart mitochondria, indicated a ratio between MAO‐A and MAO‐B, markedly different from that shown by plots of inhibition of benzylamine metabolism by various concentrations of clorgyline. The interpretation of these clorgyline plots is discussed in terms of the kinetic constants of both MAO‐A and MAO‐B, and the relative amounts of each enzyme. It is proposed that although the turnover rate constant for benzylamine metabolism by MAO‐A is much smaller than that shown by MAO‐B, in those tissues containing a large ratio of MAO‐A:MAO‐B content, the metabolism of benzylamine by MAO‐A can be detected.
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DOI: 10.1111/j.2042-7158.1980.tb13088.x
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Callingham</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:017ABE3A109660C9CE7436664445A2F6ED0A04C6</idno><date when="1980" year="1980">1980</date><idno type="doi">10.1111/j.2042-7158.1980.tb13088.x</idno><idno type="url">https://api.istex.fr/document/017ABE3A109660C9CE7436664445A2F6ED0A04C6/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">002331</idno><idno type="wicri:Area/Main/Curation">002010</idno><idno type="wicri:Area/Main/Exploration">002B68</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Some factors influencing the metabolism of benzylamine by type A and B monoamine oxidase in rat heart and liver</title><author><name sortKey="Parkinson, David" sort="Parkinson, David" uniqKey="Parkinson D" first="David" last="Parkinson">David Parkinson</name><affiliation wicri:level="4"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Pharmacology, University of Cambridge, Hills Road, Cambridge CB2 2QD</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Lyles, Geoffrey A" sort="Lyles, Geoffrey A" uniqKey="Lyles G" first="Geoffrey A." last="Lyles">Geoffrey A. 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Although under normal circumstances benzylamine appeared to be metabolized exclusively by MAO‐B in the rat liver, a contribution by both MAO‐A and a clorgyline‐resistant enzyme component was revealed when the MAO‐B activity was much reduced by pretreatment of the mitochondria with appropriate concentrations of deprenyl. These three enzyme activities also contributed to benzylamine deamination in rat heart mitochondria. However, binding studies with [3 H]pargyline, which provided an estimate of the respective concentrations of MAO‐A and MAO‐B active centres in heart mitochondria, indicated a ratio between MAO‐A and MAO‐B, markedly different from that shown by plots of inhibition of benzylamine metabolism by various concentrations of clorgyline. The interpretation of these clorgyline plots is discussed in terms of the kinetic constants of both MAO‐A and MAO‐B, and the relative amounts of each enzyme. It is proposed that although the turnover rate constant for benzylamine metabolism by MAO‐A is much smaller than that shown by MAO‐B, in those tissues containing a large ratio of MAO‐A:MAO‐B content, the metabolism of benzylamine by MAO‐A can be detected.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Angleterre de l'Est</li></region><settlement><li>Cambridge</li></settlement><orgName><li>Université de Cambridge</li></orgName></list><tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Parkinson, David" sort="Parkinson, David" uniqKey="Parkinson D" first="David" last="Parkinson">David Parkinson</name></region><name sortKey="Browne, Barbara J" sort="Browne, Barbara J" uniqKey="Browne B" first="Barbara J." last="Browne">Barbara J. Browne</name><name sortKey="Callingham, Brian A" sort="Callingham, Brian A" uniqKey="Callingham B" first="Brian A." last="Callingham">Brian A. Callingham</name><name sortKey="Lyles, Geoffrey A" sort="Lyles, Geoffrey A" uniqKey="Lyles G" first="Geoffrey A." last="Lyles">Geoffrey A. Lyles</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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