Abstract: Malate dehydrogenase-glutamate oxaloacetate
aminotransferase (MDh-GOAT) enzyme complex (the EC) was
isolated and purified from wheat and rise, their some main physicchemical
properties were studied. Michael-s constants of the EC
MDh-GOAT to malate, glutamate and NAD were investigated. This
kinetic results show a high relationship to glutamate. Taking into
account important role of the the EC in catabolism of glutamate – the
central amino acid of a nitric exchange, there is a sharp necessity of
deeper studying of this enzyme complex. Therefore the basic purpose
of the work is studying the basic physical and chemical properties of
this enzyme complex discovered by us, which would be very
important for understanding the mechanisms of reaction catalyzed by
the EC.