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. 1973 Dec;135(4):735–750. doi: 10.1042/bj1350735

The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase

Miles D Houslay 1, Keith F Tipton 1
PMCID: PMC1165890  PMID: 4778271

Abstract

1. A preparation of a partly purified mitochondrial outer-membrane fraction suitable for kinetic investigations of monoamine oxidase is described. 2. An apparatus suitable for varying the O2 concentration in a spectrophotometer cuvette is described. 3. The reaction catalysed by the membrane-bound enzyme is shown to proceed by a double-displacement (Ping Pong) mechanism, and a formal mechanism is proposed. 4. KCN, NaN3, benzyl cyanide and 4-cyanophenol are shown to be reversible inhibitors of the enzyme. 5. The non-linear reciprocal plot obtained with impure preparations of benzylamine, which is typical of high substrate inhibition, is shown to be due to aldehyde contamination of the substrate.

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Selected References

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