Properties of a ribosome-inactivating protein, gelonin, purified using three different methods.

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dc.contributor.authorSingh, Ven_US
dc.contributor.authorKar, S Ken_US
dc.date.accessioned1992-02-01en_US
dc.date.accessioned2009-05-27T09:35:38Z
dc.date.available1992-02-01en_US
dc.date.available2009-05-27T09:35:38Z
dc.date.issued1992-02-01en_US
dc.description.abstractRibosome-inactivating protein, gelonin, isolated from an Indian plant Gelonium multiflorum of Euphorbiaceae family has been used to design and synthesize immunotoxins and hormonotoxins for selective targeting purposes. Since gelonin isolated by aqueous extraction, cation-exchange chromatography and gel-filtration chromatography (Method I), contains non-proteinous material absorbing at 280 nm, the ammonium sulphate precipitation method (Method II) and Cibacron blue affinity chromatography method. (Method III) have been used to purify gelonin from the dry seeds. Three batches of gelonin purified by each method were prepared and subjected to extensive physico-chemical and immunochemical characterization. The molecular weight was determined by gel-filtration chromatography on a pre-calibrated Sephadex G-100, TSK-G4000 TW on HPLC or Superose-12 on fast protein liquid chromatography. In all cases, the molecular weight was approximately 30,000Da. The SDS-PAGE also revealed a homogeneous protein of 30kDa molecular weight. In Method II, the non-proteinous material which binds to CMC-gel in association of gelonin was substantially removed during ammonium sulphate fractionation. A careful analysis clearly revealed that Method II, although yielded low protein, gave gelonin devoid of the non-proteinous material. The SPDP modification of epsilon-NH2 groups of gelonin obtained from Methods I, II, and III was also carried out and its effect on immunoreactivity was studied.en_US
dc.description.affiliationInstitute of Self-Organising Systems and Biophysics, North-Eastern Hill University, Shillong, Meghalaya, India.en_US
dc.identifier.citationSingh V, Kar SK. Properties of a ribosome-inactivating protein, gelonin, purified using three different methods. Indian Journal of Biochemistry & Biophysics. 1992 Feb; 29(1): 31-41en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/27974
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshChromatography, Affinityen_US
dc.subject.meshChromatography, Gelen_US
dc.subject.meshPlant Proteins --chemistryen_US
dc.subject.meshPrecipitationen_US
dc.subject.meshProtein Synthesis Inhibitors --chemistryen_US
dc.subject.meshRibosome Inactivating Proteins, Type 1en_US
dc.subject.meshRibosomes --chemistryen_US
dc.subject.meshToxins, Biologicalen_US
dc.titleProperties of a ribosome-inactivating protein, gelonin, purified using three different methods.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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