Purification and Properties of a Cysteine Proteinase Occurring in Dormant Wheat Seeds

Abstract

A cysteine proteinase was purified from dormant seeds of wheat (Triticum aestivum, cultivar Norin 61) and its molecular mass was estimated to be about 23 kDa by gel filtration. The Km of this proteinase at pH 5~5 was calculated as 2 pM for Z-Phe-Arg-MCA, and its activity was inhibited by cysteine proteinase inhibitors including antipain, E-64, and leupeptin. Oryzacystatin-I, a proteinaceous cysteine proteinase inhibitor in rice seeds, also inhibited its activity.

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