Soluble and membrane-bound pig liver mitochondrial monoamine oxidase: Thermostability, tryptic digestability and kinetic properties

1972 ◽  
Vol 21 (18) ◽  
pp. 2479-2488 ◽  
Author(s):  
Lars Oreland ◽  
Bertil Ekstedt
1975 ◽  
Vol 145 (2) ◽  
pp. 311-321 ◽  
Author(s):  
M D Houslay ◽  
K F Tipton

1. The kinetics of benzylamine oxidation by a soluble preparation of rat liver mitochondrial monoamine oxidase were investigated and were shown to conform to adouble-displacement (or Ping Pong) mechanism. 2. The pathway differs in detail from that followed by other amine oxidases, including the membrane-bound enzyme in rat liver mitochondrial outer membranes. 3. It is suggested taht the conformation of the protein in the soluble state differs from that in the membrane-bound state. 4. The full rate equations for this mechanism have been deposited as Supplementary Publication SUP 50039 (5pages) at the British Library (lending Division) (formely the National Lending Library for Science and Technology), Boston Spa, Yorks, LS237BQ, U.K.. from whom copies can be obtained on the terms indicated in Biochem. J (1975) 145,5.


1973 ◽  
Vol 135 (4) ◽  
pp. 735-750 ◽  
Author(s):  
Miles D. Houslay ◽  
Keith F. Tipton

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.


1967 ◽  
Vol 242 (18) ◽  
pp. 4230-4238
Author(s):  
V. Gene Erwin ◽  
Leslie Hellerman

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