A molecularly imprinted polymeric receptor for trypsin was synthesized by employing a novel technique that is a combination of affinity separation and molecular imprinting. An enzyme-inhibitor complex of trypsin and N-acryloyl para-aminobenzamidine was polymerized with acrylamide and N,N'-methylene bis-acrylamide. Template trypsin was extracted out to obtain an affinity-imprinted polymer. Control experiments were performed to demonstrate the synergistic affinity-imprinting effect. The percentage of crosslinker used was the crucial factor in determining the imprinting efficacy of the polymers. Imprinted polymer containing 50% crosslinker exhibited a linear Scatchard plot. Unlike non-imprinted gel, the receptor exhibited almost exclusive recognition of trypsin in an individual batch experiment as well as from a mixture of trypsin and chymotrypsin.