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dc.contributor.authorSingh, Vinod-
dc.contributor.authorSingh, Ranjit C-
dc.contributor.authorDubey, Rajesh Kumar-
dc.contributor.authorAlam, Anis-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.description.abstractGelonin, a ribosome-inactivating protein has been isolated from the seeds of Gelonium multifluorum of Euphorbiaceae family by two methods and the results are compared. In method-I conventional aqueous extraction, cation-exchange and gel-filtration chromatography has been used. In method-II S-Sepharose fast now gel has been used to purify the proteins from the seed extract, followed by ammonium sulfate fractionation, cation-exchange and gel-filtration chromatography. Extensive physico-chemical and immunological characterizations show that molecular weight of gelonin as determined by gel-filtration chromatography and SDS-PAGE is -30 kDa. The non-proteinous material which binds to CMC-gel in association with gelonin in method-I is substantially removed when gelonin is purified by method-II. Cation exchange, G-100 chromatography, RP-HPLC and SDS-PAGE show that method-II yields 50% more purified gelonin when compared to the yield by method- I. The immunoreactivity of gelonin obtained by methods I and II vary from 22-26% and 50-66%, respectively and the ribosome-inactivating property vary from 46-56% and 70-87% respectively.en_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.36(4) [August 1999]en_US
dc.titlePurification and characterisation of gelonin from seeds of Gelonium multiflorumen_US
Appears in Collections:IJBB Vol.36(4) [August 1999]

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