Journal ArticleDOI
Time-dependent inhibition of monoamine oxidase by β-phenethylamine
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TLDR
Although the inhibition is time-dependent, the inactivated enzyme slowly regains activity upon removal of the beta-phenethylamine, and a model is proposed to explain the observed inhibition.About:
This article is published in Biochemical Pharmacology.The article was published on 1982-03-15. It has received 29 citations till now. The article focuses on the topics: Non-competitive inhibition & Phenethylamine.read more
Citations
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Book ChapterDOI
The new generation of monoamine oxidase inhibitors.
Cesura Andrea,Alfred Pletscher +1 more
TL;DR: In subjects with Parkinson's disease the MAO-B inhibitor L-deprenyl exerts a L-dopa-sparing effect, prolongs L- dopa action and seems to have a favorable influence regarding on-off disabilities.
Journal ArticleDOI
Assessment of Enzyme Inhibition: A Review with Examples from the Development of Monoamine Oxidase and Cholinesterase Inhibitory Drugs
Rona R. Ramsay,Keith F. Tipton +1 more
TL;DR: Key principles and approaches for the reliable determination of enzyme activities and inhibition as well as some of the methods that are in current use for such studies with these two enzymes are described.
Journal ArticleDOI
Interactions of monoamine oxidase with substrates and inhibitors.
Journal ArticleDOI
Human platelet monoamine oxidase—A useful enzyme in the study of psychiatric disorders?
Journal ArticleDOI
The nature of the inhibition of rat liver monoamine oxidase types A and B by the acetylenic inhibitors clorgyline, l-deprenyl and pargyline☆
TL;DR: The kinetics of inhibition of rat liver mitochondrial monoamine oxidase by clorgyline, l-deprenyl and pargyline are consistent with a mechanism whereby a reversible interaction between the inhibitor and the enzyme active site under conditions of thermodynamic equilibrium is followed by a time-dependent formation of the covalently-bound enzyme-inhibitor adduct.
References
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Journal ArticleDOI
A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
TL;DR: The original Lowry method of protein determination has been modified by the addition of sodium dodecyl sulfate in the alkali reagent and an increase in the amount of copper tartrate reagent to be used with membrane and lipoprotein preparations without prior solubilization or lipid extraction.
Journal ArticleDOI
Monoamine oxidase—I: Specificity of some substrates and inhibitors
TL;DR: The effects of hydrogen-ion concentration on enzyme activity are consistent with the view that unprotonated amines are the species which bind to the enzyme, and led to formulation of a proposed mechanism of dehydrogenation which does not depend upon intermediate formation of Schiff base from the substrate amine.
Journal ArticleDOI
A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes.
Miles D. Houslay,Keith F. Tipton +1 more
TL;DR: A preparation of mitochondrial outer membranes from rat liver can be shown to contain two kinetically distinct monoamine oxidase activities, distinguishable by their different sensitivities to the irreversible inhibitor clorgyline and by the effect of the reversible inhibitors benzyl cyanide and 4-cyanophenol.
Journal ArticleDOI
The nature of the electrophoretically separable multiple forms of rat liver monoamine oxidase.
Miles D. Houslay,Keith F. Tipton +1 more
TL;DR: Treatment of a partly purified preparation of rat liver monoamine oxidase with the chaotropic agent sodium perchlorate caused the enzyme to migrate as a single band of activity of polyacrylamide-gel electrophoresis, whereas the untreated enzyme separated into a number of bands.
Journal ArticleDOI
Kinetics of suicide substrates.
TL;DR: Equations for the rate of inactivation have been derived and integrated to obtain equations describing progress curves and the steady-state hypothesis is applicable when catalytic quantities of enzyme are used.