The kinetic parameters of beef heart cytoplasmic and pig heart mitochondrial malate dehydrogenases have been examined over a wide range of enzyme concentration. No significant changes are observed in these properties. In conjunction with active enzyme sedimentation and sedimentation equilibrium experiments, it is concluded that there is no evidence for dissociation of the dimeric enzyme at any enzyme level in the kinetic analyses. Thus, if dissociation occurs, it must be too slow to be of significance in determining the kinetic properties of the enzyme. It is shown that unless a subunit and its dimeric form have identical kinetic and substrate binding characteristics, the kinetic parameters should change as a function of enzyme concentration.
|Number of pages||5|
|Journal||Journal of Biological Chemistry|
|State||Published - 1978|