Purification of trypsin by affinity chromatography with sulphamethoxazolum ligand

Pharmaceuticals have already been studied comprehensively both in their physico-chemical properties and their biological effect. Most of these compounds are chemically synthesized and less susceptible to degradation by micro-organism or suffering from solvent effect compared with the bio-active substances. Affinity chromatographic columns composed of pharmaceutical compounds as the ligand should have advantages such as long life, low cost and low toxicity. This paper describes the preparation of sulphamethoxazolum immobilized on silica as the column packing and the study of its interactions with proteins and enzymes. It was found that this material showed an affinity specific to trypsin with a dissociation constant of around 10(-6) M. The enzymatic activity of commercial trypsin can be increased by a factor of ten after purification with such a column.