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Monoamine oxidase in Tribolium confusum Duval

K.D. Chaudhary
André Lemonde
Uma Srivastava
KC

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K.D. Chaudhary

Résumé du colloque

In the present investigation we have determined the activity of MAO during the growth and metamorphosis of T. Confusum. We have also studied certain biochemical characteristics of this enzyme in the total homogenate. Zero-order reaction occurs for 40 minutes, with 6.29 x 10^-9 M final concentration of 14C-tryptamine at an optimum pH of 7.5. Michaelis constant (Km) under the optimal conditions is 8.7 x 10^-3 M. Maximum enzyme activity is obtained at 37ºC and the activation energy (E) is 10, 440 cal/mole, within the limits of optimum temperature. At optimum concentrations, Ni, Zu, Co and Mn activate the enzyme considerably. Harmine and parmate inhibit the enzyme. As in mammalian systems MAO activity is firmly bound to the mitochondrial fraction.

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Section :
Biochimie
news icon Thème du colloque :
Biochimie
manager icon Responsables :
Édouard Pagé
host icon Hôte : Université Laval

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