Interaction of NAD-dependent dehydrogenases with human erythrocyte membranes. Evidence that D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase are catalytically active in a membrane-bound state.
Interaction of D-glyceraldehyde-3-phosphate dehydrogenase (GPDH) and lactate dehydrogenase with human erythrocyte membranes was studied. Under the conditions of low ionic strength, both enzymes bound to the membranes with similar affinities (kd = 1 microM). The binding was accompanied by complete inhibition of GPDH and by a 65-75% inhibition of lactate dehydrogenase (LDH). Increasing the ionic strength to physiologically meaningful values (0.15 M) completely abolished the inactivation of both dehydrogenases in the presence of erythrocyte membranes, but did not preclude their binding. These results suggest that different modes of enzyme-membrane interaction can be realized under the conditions of low and high ionic strength. They also indicate that GPDH and LDH are capable of functioning in a membrane-bound state.
Muronetz
V I
VI
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia. muric@fac.genebee.msu.su
Shcherbatova
N A
NA
Nagradova
N K
NK
D000818:Animals; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D013552:Swine
D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases