Physico-chemical evidence for the interaction between aldolase and glyceraldehyde-3-phosphate dehydrogenase.
Polarization of fluorescence measurements of aldolase and D-glyceraldehyde-3-phosphate dehydrogenase labeled with fluorescein isothiocyanate have been used to detect the possible formation of a soluble complex between the proteins. The results suggest an interaction between aldolase and D-glyceraldehyde-3-phosphate dehydrogenase with an apparent dissociation constant 3 X 10(-7) M and an apparent stoichiometry of two aldolase tetramers bound per tetramer of D-glyceraldehyde-3-phosphate dehydrogenase.
D005452:Fluoresceins; D005634:Fructose-Bisphosphate Aldolase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D007700:Kinetics; D013050:Spectrometry, Fluorescence; D013861:Thiocyanates
D005452:Fluoresceins; D013861:Thiocyanates; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005634:Fructose-Bisphosphate Aldolase