Primary structure of β-momorcharin, a ribosome-inactivating protein from the seeds of Momordica Charantia Linn (Cucurbitaceae)
✍ Scribed by Ye; Guo-Jie; Lu; Bao-Yuan; Jin; Shan-Wei; Qian; Rui-Qing; Wang; Yu
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 687 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0256-7660
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✦ Synopsis
a ribosome-inactivating protein from the seeds Momordica Charantia Linn ( Cucurbitaceae ) of Abstrsct The complete amino acid sequence of ~momorcharh, a ribosome-inactivating p t e i n from the seeds of Morn& &rrantia Linn ( Cucurbiteceae) has been determined. 'Ihis has been done by the sequence analysis of pepides obtained by enymatic digestion with w i n , chynmtq-psin and S . w e u s V8 protease, as well as by chemical cleavage with BNPSskatole. The protein consists of 249 amino acid residues containing one asparapelinked sugar p u p attached to the site of Asn 5 1 and has a calculated relative molecular mass of 28,452 Da without addition of the carbohydrate. Comparison of this sequence with those of hichosanthin and other r i h i n a c t i v % pmteins &om different species of plants shows a signircant homology with each other.
Regarding the similarity of their biological proprties, an active domain of thesz proteins has been predicted hen:.
Keymwds
Momorcharin, ribommeinactivating protein (RIP), primary struchm, sequence comparison