V. Cheriyath et al., Purification and characterization of a poly(A)-binding protein from chickpea (Cicer arietinum) epicotyl, I J BIOCH B, 37(2), 2000, pp. 107-113
A poly(A)-binding protein (PABP) with mol wt 72,000 has been purified from
chickpea (Cicer arietinum) epicotyls by ammonium sulfate fractionation, Cib
acron blue F3-GA and poly(A) agarose chromatography. The binding properties
and the specificity of binding show that the purified protein is an analog
ue of PABPs in other eukaryotes. This PABP is highly susceptible to proteol
ysis and upon degradation forms a polypeptide fragment of mol wt 21,000 whi
ch has an independent poly(A) binding activity.