A raw extractof 4 days old teosinte coleoptiles (Zea diploperennis) was prepared in a phosphates buffer saline (PBS), pH 7.2, 0.15 M., in which was identified and quantified lectin and β-glucosidase activities.The electrophoretic pattern SDS-PAGE of the raw extract presented a complex of components to stand out a component of 60 kDa. The same raw extract on a two-dimensional analysis, showed a map of morethan 50 proteins dots.
Lectin and β-glucosidase of teosinte coleoptiles were partially purified from the raw extract. Lectin was purified by affinity chromatography on Sheparose- lactose, andβ-glucosidase by ionic exchange. Lectin and β-glucosidase activities were determined in the same samples. Electrophetic analysis in SDS-PAGE presented a band of 60 kDa corresponding to β-glucosidase enzyme(according to data reported in maize coleoptiles) followed by a band of 58 kDa, wich suggests is the lectin in teosinte. The native-PAGE electrophoretic analysis of this same fraction from purifiedlectin gave a similar pattern to that reported by Martinez et al (2004) in the CCL with a weight of 132 kDa. The two-dimensional analysis of this fraction presented two spots with isoelectric point of theorder of 8 and 8.3 and molecular masses of 60 and 58 kDa respectively, which confirms the result of this fraction analysis in SDS-PAGE. The above data are similar to that of β-glucosidase of teosintereported by Alonso et al (doctoral thesis in progress, 2010).
The electrophoretic pattern of the preparation of β-glucosidase showed a semipurified fraction, where a component of the order of 66 kDa,was more meaningful, and this component corresponds to β-glucosidase of teosinte, which was corroborated by amino acid sequence data in other performed experiments (data not shown here). The...