Purification and characterization of a poly(A)-binding protein from chickpea (Cicer arietinum) epicotyl

Citation
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
Citations number
28
Categorie Soggetti
Biochemistry & Biophysics
Journal title
INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS
ISSN journal
03011208 → ACNP
Volume
37
Issue
2
Year of publication
2000
Pages
107 - 113
Database
ISI
SICI code
0301-1208(200004)37:2<107:PACOAP>2.0.ZU;2-Z
Abstract
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.