Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/19817
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dc.contributor.authorCheriyath, Venugopalan-
dc.contributor.authorBalasubrahmanyam, A-
dc.contributor.authorKapoor, Harish C-
dc.date.accessioned2013-07-16T07:12:18Z-
dc.date.available2013-07-16T07:12:18Z-
dc.date.issued2000-04-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/19817-
dc.description107-113en_US
dc.description.abstractA poly(A)-binding protein (PABP) with mol wt 72,000 has been purified from chickpea (Cicer arietinum) epicotyls by ammonium sulfate fractionation , Cibacron blue F3-GA and poly(A) agarose chromatography. The binding properties and the specificity of binding show that the purified protein is an analogue of PABPs in other eukaryotes. This PABP is highly susceptible to proteolysis and upon degradation forms a polypeptide fragment of mol wt 21,000 which has an independent poly(A) binding activity.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rightsCC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.37(2) [April 2000]en_US
dc.titlePurification and characterization of a poly(A)-binding protein from chickpea (Cicer arietinum) epicotylen_US
dc.typeArticleen_US
Appears in Collections: IJBB Vol.37(2) [April 2000]

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