Interaction of polymeric derivatives of trypsin with its protein inhibitor

Trypsin and its inhibitor (ovomucoid from duck egg whites) were immobilized on water-soluble polymers. The activities of immobilized proteins were found to be controlled by the nature of the polymer chain. Immobilization on a flexible-chain polyacrylamide resulted in the decreased activity of the immobilized proteins because of the intramolecular association of their molecules. Polymer chains did not give rise to any additional steric hindrances for the interaction of the immobilized proteins with their substrates. When the proteins were immobilized on rigid-chain dextrans with different chain lengths, the activity of immobilized proteins was fully retained. In addition, the interaction between the immobilized enzyme and the immobilized inhibitor could be controlled.