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

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概要

• 論文の詳細を見る

• A comparison of haemoglobin, 2,4-dinitrophenyl and N,O-dibenzyloxycarbonyl-tyrosine as ligands for the affinity chromatography of wheat-leaf proteinases delete with 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.

• 日本植物生理学会の論文

著者

• Dalling M.j.

  Plant Science Section School Of Agriculture And Forestry University Of Melbourne

• Frith G.j.t.

  Plant Science Section School Of Agriculture And Forestry University Of Melbourne

• Swinden L.B.

  Plant Sciences Section, School of Agriculture and Forestry, University of Melbourne

• Swinden L.b.

  Plant Sciences Section School Of Agriculture And Forestry University Of Melbourne

関連論文

• Proteolytic enzymes in green wheat leaves I. Isolation on DEAE-cellulose of several proteinases with acid pH optima
• Proteolytic enzymes in green wheat-leaves III. Inactivation of acid proteinase II by diazoacetyl-DL-norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)-propane
• Proteolytic enzymes in green wheat leaves II. Puriflcation by affinity chromatography, and some properties of proteinases with acid pH optima

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