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Balsamin, a novel ribosome-inactivating protein from the seeds of Balsam apple Momordica balsamina

Kaur, Inderdeep, Yadav, Santosh K., Hariprasad, Gururao, Gupta, R. C., Srinivasan, Alagiri, Batra, Janendra K. and Puri, Munish 2012, Balsamin, a novel ribosome-inactivating protein from the seeds of Balsam apple Momordica balsamina, Amino acids, vol. 43, no. 2, pp. 973-981.

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Title Balsamin, a novel ribosome-inactivating protein from the seeds of Balsam apple Momordica balsamina
Formatted title Balsamin, a novel ribosome-inactivating protein from the seeds of Balsam apple Momordica balsamina
Author(s) Kaur, Inderdeep
Yadav, Santosh K.
Hariprasad, Gururao
Gupta, R. C.
Srinivasan, Alagiri
Batra, Janendra K.
Puri, Munish
Journal name Amino acids
Volume number 43
Issue number 2
Start page 973
End page 981
Total pages 9
Publisher Springer Wien
Place of publication Vienna, Austria
Publication date 2012-08
ISSN 0939-4451
1438-2199
Keyword(s) balsamin
cucurbitaceae
momordica balsamina
ribosome inactivating protein (RIP)
RNA N-glycosidase
Summary Plant seeds, a rich source of proteins, are considered important for their application as functional ingredients in a food system. A novel ribosome-inactivating protein (RIP), balsamin was purified from the seeds of Balsam apple, Momordica balsamina. Balsamin was purified by ion exchange chromatography on CM Sepharose and gel filtration on superdex-75. It has a molecular weight of 28 kDa as shown by SDS-PAGE analysis. Balsamin inhibits protein synthesis in a rabbit reticulocyte lysate-based cell free translation assay with an IC50 of 90.6 ng ml−1. It has RNA N-glycosidase activity and releases a 400-base long fragment termed the Endo fragment from 28S rRNA in the same manner as does saporin-6 from Saponaria officinalis. The N-terminal sequence analysis of the first 12 amino acids of balsamin revealed that it shares 83% similarity with type I RIP α-MMC from Momordica charantia and 50% similarity with β-MMC (from Momordica charantia), bryodin I (from Bryonia dioica) and luffin a (from Luffa cylindrica). Balsamin was further characterized by mass spectrometry. CD spectroscopic studies indicate that secondary structure of balsamin contains helix (23.5%), β-strand (24.6%), turn (20%) and random coil (31.9%). Thus RIPs activity expressed in vegetables like Momordica sp. advocates its usage in diet.
Language eng
Field of Research 100302 Bioprocessing, Bioproduction and Bioproducts
060107 Enzymes
030401 Biologically Active Molecules
Socio Economic Objective 860105 Nutraceuticals and Functional Foods
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2011, Springer-Verlag
Persistent URL http://hdl.handle.net/10536/DRO/DU:30044234

Document type: Journal Article
Collection: Centre for Biotechnology and Interdisciplinary Sciences (BioDeakin)
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