Purification and characterization of a lectin from seeds of Vatairea macrocarpa Duke
1998
Cavada, B.S. | Santos, C.F. | Grangeiro, T.B. | Nunes, E.P. | Sales, P.V.P. | Ramos, R.L. | Sousa, F.A.M. de | Crisostomo, C.V. | Calvete, J.J.
A lectin from Vatairea macrocarpa Duke seeds (VML) was isolated using affinity chromatography on a guar gum column. The lectin, a glycoprotein without erythrocyte specificity, displays specificity to galactose and some derivatives. On SDS-polyacrylamide gels, V. macrocarpa seed lectin is composed of two major high-Mr bands of 34 and 32 kDa and two minor low-Mr bands of 22 and 13 kDa. N-Terminal sequencing showed that the 34, 32, and 13 kDa products possess identical N-terminal sequence, which display best similarity with the N-terminal portion of Robinia pseudoacacia lectins (RPL). On the other hand, the N-terminal sequence of the 22 kDa band can be aligned with an internal sequence of RPL starting at residue 149 of the cDNA-derived sequence. These data indicate that, like other leguminous lectins, VML is made up of a mixture of one-chain 30-35 kDa glycoforms and of 22 and 13 kDa endogenous C- and N-terminal fragments. Size-exclusion chromatography indicated that, at neutral pH, VML is predominantly a dimeric (70 kDa) protein, although tetramers (115 kDa) and larger aggregates (300 kDa) were also present.
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