Purification and characterization of a 29 kDa poly(A)-binding protein from chickpea (Cicer arietinum) epicotyl.
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.
Cheriyath
V
V
Division of Biochemistry, Indian Agricultural Research Institute, New Delhi.
Balasubrahmanyam
A
A
Kapoor
H C
HC
D029863:Cicer / Q000737:chemistry*; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D010946:Plants, Medicinal; D039102:Poly(A)-Binding Proteins; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification*
D010940:Plant Proteins; D039102:Poly(A)-Binding Proteins; D016601:RNA-Binding Proteins