Analysis of the lectins from teosinte (Zea diploperennis) and maize (Zea mays) coleoptiles.

To identify molecular evidence of the common origin of maize and teosinte, a lectin from teosinte coleoptile (TCL) was purified, through affinity chromatography on a lactosyl-Sepharose column, and some of the physicochemical parameters were compared with those from the maize coleoptile lectin (CCL). TCL is a 92 kDa glycoprotein constituted mainly by aspartic, glutamic, glycine, leucine, and lysine residues; in minor proportion, methionine and cysteine were also found. The glycannic portion of the lectin, which corresponds to 10% w/w, is composed by Gal, Man, and GlcNAc. CCL is an 88.7 kDa glycoprotein that contains 12% sugars by weight; its sugar and amino acid compositions are similar to those of TCL. TCL is formed by two isoforms identified through acidic electrophoresis, whereas CCL is constituted by a single molecular form. The NH(2) termini of both TCL isoforms are blocked, but their amino acid sequences determined from tryptic peptides by matrix-assisted laser desorption ionization time-of-flight) indicated that TCL isoforms have no homology with other mono- or dicotyledonous lectins, including CCL. TCL, just as CCL, showed hemagglutinating activity toward animal erythrocytes, including human A, B, and O. Hapten inhibition assays indicated that although TCL shows broader sugar specificity than CCL, it recognizes Gal in O- and N-glycosidically linked glycans. Both lectins are equally well recognized by antibodies against TCL.