luffin/momordica

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GreinarKlínískar rannsóknirEinkaleyfi

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Chemical modifications of momordin-a and luffin-a, ribosome-inactivating proteins from the seeds of Momordica charantia and Luffa cylindrica: involvement of His140, Tyr165, and Lys231 in the protein-synthesis inhibitory activity.

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Effects of chemical modifications on the protein-synthesis inhibitory (PSI) activities of momordin-a and luffin-a were investigated. Treatment with a 50-fold excess of diethylpyrocarbonate at pH 6.5 modified one histidine residue in momordin-a and luffin-a and reduced their PSI activities to 10% and

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

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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

Proteins with abortifacient, ribosome inactivating, immunomodulatory, antitumor and anti-AIDS activities from Cucurbitaceae plants.

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1. The biochemical characteristics and biological activities of eight Cucurbitaceae plant proteins designated trichosanthin (isolated from tubers of Trichosanthes kirilowii), beta-trichosanthin (isolated from tubers of Trichosanthes cucumeroides), alpha- and beta-momorcharins (isolated from seeds of

Purification and characterization of charantin, a napin-like ribosome-inactivating peptide from bitter gourd (Momordica charantia) seeds.

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A peptide designated charantin, with a molecular mass of 9.7 kDa, was isolated from bitter gourd seeds. The procedure comprised affinity chromatography on Affi-gel blue gel, ion-exchange chromatography on Mono S and gel filtration on Superdex 75. The N-terminal sequence of charantin exhibited marked

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Herbal & Natural Medicine

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