Proteolytic enzymes in green wheat leaves II. Purification by affinity chromatography, and some properties of proteinases with acid pH optima

摘要

A comparison of haemoglobin, 2,4-dinitrophenyl and N,O-dibenzyloxycarbonyltyrosine as ligands for the affinity chromatography of wheat-leaf proteinases delete widi acid pH optima, established that haemoglobin was the most satisfactory. Using haemoglo-bin-Sepharose 4B affinity chromatography it was possible to purify wheat-leaf acid proteinases, previously isolated on DEAE-cellulose, to homogeneity as judged by polyacrylamide gel electrophoresis. Some properties of three purified proteinases are presented and discussed.