Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/24985
Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Purification and characterization of thaumatopain, a cysteine protease from the arils of the plant Thaumatococcus daniellii
Authors: Cusack, Maggie
Stephen, Andrew G
Powls, Roy
Beynon, Robert
Contact Email: maggie.cusack@stir.ac.uk
Issue Date: Feb-1991
Citation: Cusack M, Stephen AG, Powls R & Beynon R (1991) Purification and characterization of thaumatopain, a cysteine protease from the arils of the plant Thaumatococcus daniellii, Biochemical Journal, 274 (1), pp. 231-236.
Abstract: Aqueous extracts of the aril of the seed of Thaumatococcus daniellii contain, in addition to the intensely sweet protein thaumatin, a cysteine protease that we have termed thaumatopain. Thaumatopain has been purified by ion-exchange chromatography from arils, and is a monomeric protein of M(r) 30000. The protease strongly resembles papain in proteolytic activity, pH optima, susceptibility to inhibitors of cysteine proteases and in N-terminal sequence. The protease has also been identified in crude aril extracts by affinity labelling with iodo[14C]acetate. Thaumatopain is responsible for the cysteine protease activity previously attributed to thaumatin. Thaumatin is digested by thaumatopain at neutral to alkaline pH values.
DOI Link: http://dx.doi.org/10.1042/bj2740231
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