Proteolytic enzymes in green wheat leaves II. Purification by affinity chromatography, and some properties of proteinases with acid pH optima
- 1 September 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 19 (6) , 1029-1041
- https://doi.org/10.1093/oxfordjournals.pcp.a075669
Abstract
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.Keywords
This publication has 1 reference indexed in Scilit:
- The gel-filtration behaviour of proteins related to their molecular weights over a wide rangeBiochemical Journal, 1965