Chymotrypsin is a prominent member of the family of serine proteases. The present studies demonstrate the presence of a native fragment contain-ing 14 residues from Ile16 to Trp29 in a-chymotrypsin that binds to chy-motrypsin at the active site with an exceptionally high affinity of ± ·10 )11 mand thus works as a highly potent competitive inhib-itor. The commercially available a-chymotrypsin was processed through a three phase partitioning system (TPP). The treated enzyme showed consid-erably enhanced activity. .
