Complexes of polyelectrolytes with the enzymes pepsin and α-chymotrypsin

It was shown that both the enzymes pepsin and α‐chymotrypsin will displace the anionic dye Eosin Y from complexes of the dye with the polycations protamine or polybrene. The dyerelease was monitored fluorimetrically and was found to be strongly time‐dependent. At equilibrium, pepsin released all the bound dye from both polycation‐dye complexes when the mole ratio of pepsin to base moles of polycation were 1 : 10 for protamine and 1 : 13 for polybrene. α‐Chymotrypsin did not release all the bound dye, but appeared to form definite complexes with the polycations. The existence of the complexes between the enzymes and the polycations was correlated with the fact that the polycations are inhibitors of the enzymes. Additionally, it has been shown that pepsin releases Acridine Orange (AO) from a poly(vinyl sulfate) (PVS)‐AO complex. The mole ratio of pepsin to base moles of PVS was found to be 1 : 2,5. Cooperative binding constants were also evaluated for each dye‐polyion system.