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The study of ubiquitin-dependent increase in monoamine oxidase sensitivity to proteolysis and specific inhibitor, pargyline

The study of ubiquitin-dependent increase in monoamine oxidase sensitivity to proteolysis and specific inhibitor, pargyline,10.1134/S1990750809020048,

The study of ubiquitin-dependent increase in monoamine oxidase sensitivity to proteolysis and specific inhibitor, pargyline  
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Insertion of exogenous ubiquitin into rat brain mitochondria in the presence of ATP and the ATPregenerating system (creatine phosphate/creatine phosphokinase) results in the increase in: sensitivity of mitochondrial monoamine oxidases (MAO) A and B to inhibition by mechanism based inhibitor and incorporation of [3H]-pargyline, which was especially notable in the fraction obtained by immunoprecipitation of mitochondrial proteins with anti-ubiquitin antiserum and protein A Sepharose. This suggests that MAO is a potential substrate for ubiquitination in vitro. However, the content of the tritium label in this fraction was less than 0.1 % and not more than 0.25% of total radioactivity of [3H]-pargyline bound to control and ATP-ubiquitin treated mitochondria, respectively. Insertion of ubiquitin into mitochondria did not influence molecular masses of [3H]-pargyline labeled proteins. These results suggest that direct ubiquitination of MAO insignificantly contributes to marked changes in the sensitivity of MAO A and MAO B to proteolysis and specific inhibition found under these experimental conditions. It is possible that more complex processes are involved into realization of these effects during ATP-dependent ubiquitin incorporation into mitochondria.
Journal: Biochemistry (moscow) Supplement Series B: Biomedical Chemistry , vol. 3, no. 2, pp. 145-148, 2009
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