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Purification and characterization of a 29 kDa poly(A)-binding protein from chickpea (Cicer arietinum) epicotyl.
Indian J Biochem Biophys ; 2001 Aug; 38(4): 258-62
Article in English | IMSEAR | ID: sea-26841
ABSTRACT
A poly(A)-binding protein (PABP) with mol wt 29,000 has been purified from chickpea (Cicer arietinum) epicotyl by ammonium sulfate fractionation and Cibacron blue F3-GA chromatography, making a complex with poly(A) and elution of PABP-poly(A) complex at 45 degrees C from oligo d(T)-cellulose. The elution pattern and binding properties show that the purified protein is different from the PABP (mol. wt 72,000) reported earlier from our laboratory.
Subject(s)
Full text: Available Index: IMSEAR (South-East Asia) Main subject: Plant Proteins / Plants, Medicinal / RNA-Binding Proteins / Cicer / Poly(A)-Binding Proteins / Molecular Weight Language: English Journal: Indian J Biochem Biophys Year: 2001 Type: Article

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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Plant Proteins / Plants, Medicinal / RNA-Binding Proteins / Cicer / Poly(A)-Binding Proteins / Molecular Weight Language: English Journal: Indian J Biochem Biophys Year: 2001 Type: Article