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
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概要
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Acid proteinase II isolated from green wheat leaves in a purified form was rapidly inactivated at pH=5.5 to 6.0 by a 50-fold molar excess of diazoacetyl-DL-norleucine methyl ester (DAN) in the presence of cupric ions which were essential for inactivation. The acid proteinase was also inactivated by reaction with 1,2-epoxy-3-(p-nitrophenoxy)-propane (EPNP). The inactivation by EPNP was much slower than by DAN and the half-life of the activity was 24 hr.
- 日本植物生理学会の論文
著者
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Dalling M.j.
Plant Sciences Section School Of Agriculture And Forestry University Of Melbourne
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Dalling M.j.
Plant Science Section School Of Agriculture And Forestry University Of Melbourne
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Frith G.j.t.
Plant Sciences Section School Of Agriculture And Forestry University Of Melbourne
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Frith G.j.t.
Plant Science Section School Of Agriculture And Forestry University Of Melbourne
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Peoples M.B.
Plant Sciences Section, School of Agriculture and Forestry, University of Melbourne
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Peoples M.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