PA2 albumins from five different cultivars of kabuli-type chickpea and
from one pea cultivar have been purified and characterized. Selective
extraction of albumins was followed by two gel filtration purificatio
n steps. In all chickpea cultivars, PA2 is made up of one type of prot
ein while pea PA2 is made up of two isoforms as observed by nondenatur
ating PAGE. PA2 has so far no defined function in pea while in chickpe
a a similar protein to PA2 has been described as a lectin. The present
study confirms that PA2 from pea and chickpea agglutinates papainized
human erythrocytes. Also it is reported that chickpea and pea PA2 are
allergens for individuals sensitive to chickpea intake.