Balsmin, a novel ribosome inactivating protein purified from the seeds of Balsam Apple (Momordica balsamina).

Inderdeep Kaur, Santosh Yadav, Gururao Hariprasad, Raghbir Gupta, Alagiri Srinivasan, Janendra Batra, Munish Puri

    Research output: Contribution to journalArticle

    20 Citations (Scopus)

    Abstract

    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 fromthe seeds of Balsamapple, 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 shares83%similarity with type I RIP a-MMC from Momordica charantia and 50% similarity with b-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%), b-strand (24.6%), turn (20%) and random coil (31.9%). Thus RIPs activity expressed in vegetables like Momordica sp. advocates its usage in diet.

    Original languageEnglish
    Pages (from-to)973-981
    Number of pages9
    JournalAMINO ACIDS
    Volume43
    Issue number2
    DOIs
    Publication statusPublished - 2012

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