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Tonin was purified from rat submaxillary gland homogenates by affinity chromatography on soybean trypsin inhibitor coupled CH-Sepharose 4B and two additional steps of conventional chromatography. The use of affinity chromatography by soybean trypsin inhibitor coupled CH-Sepharose 4B permits a new approach in the purification of tonin, since it can completely separate in one step troublesome contamination of the enzymes which showed tosyl-L-arginine methyl ester hydrochloride esterase activity. Tonin is purified 11-fold to a homogeneous state on polyacrylamide gel electrophoresis at a yield of 21%.
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