Upon electrophoresis of Con-A, LCA-A, LCA-B and LCA at pH8.6, minor anodic components, which had no affinity for lectin-reactive AFP, were found in some lectin preparations. Time-dependent increase in electrophoretic mobility, spreading of electrophoretic band and loss of affinity for AFP were observed particularly with E-PHA when the lectin was dissolved in buffer at pH8.6 and kept at 4°C. These changes of E-PHA and the formation of minor bands of other lectins were reduced by lowering the pH to 7.5 and minimized by the presence as low as 0.1mM each of MnCl
2, CaCl
2 and MgCl
2. LCA preparations were relatively stable at pH8.6 without added divalent cations. Lot to lot variations in electrophoretic mobility and affinity for AFP were found with LCA-B. Heterogeneity of subunit composition was also present in some lectins. Subunit molecular weights for the common and major component for each lectin, determined in the present study, were 27, 500 for Con-A, 19, 500 for LCA-A and 30, 000 for E-PHA. Lectin-reactive AFP was suggested as a simple and sensitive measure for quality control of lectins. Conversely, those variabilities of lectins should be taken into account in lectin-affinity electrophoresis of glycoproteins.
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