Purification of tonin by chromatography using soybean trypsin inhibitor coupled CH-sepharose 4B.
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%.
D000327:Adsorption; D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration; D008297:Male; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification*; D011134:Polysaccharides / Q000494:pharmacology*; D011506:Proteins; D051381:Rats; D011919:Rats, Inbred Strains; D012685:Sepharose / Q000494:pharmacology*; D013363:Submandibular Gland / Q000032:analysis; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000494:pharmacology*; D014361:Trypsin Inhibitors / Q000494:pharmacology*
D011134:Polysaccharides; D011506:Proteins; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D014361:Trypsin Inhibitors; D012685:Sepharose; D007703:Peptidyl-Dipeptidase A