M. Kino et al., PURIFICATION AND CHARACTERIZATION OF 3 MITOGENIC LECTINS FROM THE ROOTS OF POKEWEED (PHYTOLACCA-AMERICANA), Bioscience, biotechnology, and biochemistry, 59(4), 1995, pp. 683-688
Three mitogenic lectins, designated PL-A, PL-B, and PL-C, were purifie
d from the roots of pokeweed (Phytolacca americana) using Q-Sepharose
column chromatography followed by gel filtration on Sephadex G-75, hyd
rophobic chromatography on Butyl-Toyopearl, and FPLC on a Mono-Q colum
n. PL-A, PL-B, and PL-C are acidic proteins having isoelectric points
of 4.35 and their apparent molecular masses were 22, 48, and 21kDa by
SDS-polyacrylamide gel electrophoresis in the presence of 2-mercaptoet
hanol, respectively, The three lectins have similar amino acid composi
tions rich in half-cystine and similar N-terminal sequences, indicatin
g that they are homologous proteins, Identical sequences of N-terminal
regions and six corresponding tryptic peptides in PL-A and PL-B sugge
sted that PL-A may be an N-terminal half fragment of PL-B. Although al
l of three lectins have mitogenic activities, PL-B is a mitogenic lect
in with the most potent hemagglutinating and mitogenic activities, and
PL-C has almost no hemagglutinating activity.