Bovine α- and β-trypsin were separated by affinity chromatography on a column of chicken ovomucoid covalently bound to Sepharose. The two active fractions were selectively eluted by a pH gradient. The procedure was also applied to the purification of porcine and dogfish trypsins and to the isolation of trypsin from activated bovine pancreatic juice. Neither trypsinogen nor a-chymotrypsin was retarded by this column.
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