Chemical modification of cystein 149 residues from yeast apo-glyceraldehyde-3-phosphate dehydrogenase either by iodoacetamidonaphtol or N-(4-dimethylamino-3,5-dinitrophenyl) maleimide results in the disappearance of free sulfhydryl groups according to "full sites reactivity", whereas loss of the dehydrogenase activity occurs following "half of the sites reactivity". Chemical modification of the same cystein residues of the rabbit muscle apoenzyme by N-(4-dimethylamino-3,5-dinitrophenyl) maleimid shows that both loss of activity and disappearance of the sulphydryl groups may be described as "full sites reactivity" phenomena. After chemical modification by iodoacetamidonaphtol both processes follow "half of the sites reactivity".