Estimation of monoamine oxidase concentrations in soluble and membrane-bound preparations by inhibitor binding.
A modification of the [3H]-pargyline labelling technique is presented for determining the active-site concentration of monoamine oxidase in soluble preparations. Kinetic considerations show that the rate of reaction of MAO-A with low concentrations of free pargyline will be very much slower than that of MAO-B. Failure to use adequate reaction times for the concentration of pargyline added can lead to gross underestimation of the quantity of MAO-A present.
Anderson
M C
MC
Department of Biochemistry, Trinity College, Dublin, Ireland.
Tipton
K F
KF
D000818:Animals; D002417:Cattle; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008995:Monoamine Oxidase / Q000378:metabolism*; D009994:Osmolar Concentration; D010293:Pargyline / Q000378:metabolism; D012995:Solubility; D013997:Time Factors
D010293:Pargyline; D008995:Monoamine Oxidase