STORRE
STORRE: Stirling Online Research Repository
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 |
| Author(s): | Cusack, Maggie Stephen, Andrew G Powls, Roy Beynon, Robert |
| Contact Email: | maggie.cusack@stir.ac.uk |
| Issue Date: | Feb-1991 |
| Date Deposited: | 23-Feb-2017 |
| 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. https://doi.org/10.1042/bj2740231 |
| 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: | 10.1042/bj2740231 |
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| Licence URL(s): | http://www.rioxx.net/licenses/under-embargo-all-rights-reserved |
| File | Description | Size | Format | |
|---|---|---|---|---|
| 231.full.pdf | Fulltext - Published Version | 1.32 MB | Adobe PDF | Under Embargo until 2999-12-16 Request a copy |
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