ONE-STEP PURIFICATION OF THE BETA-GLUCAN ELICITOR-BINDING PROTEIN FROM SOYBEAN (GLYCINE-MAX L) ROOTS AND CHARACTERIZATION OF AN ANTIPEPTIDEANTISERUM

A low abundance beta-glucan elicitor-binding protein from soybean was isolated by a rapid, simple and one-step purification method yielding about 9000-fold enrichment, The affinity-based purification technique was more efficient than a procedure that uses conventional methods and preserved the binding activity to a much larger extent, The final pre paration consisted of one major protein with an apparent molecular mas s of about 75 kDa, Electrophoretic analyses of the purified and photoa ffinity-labeled binding protein showed that the native protein was an oligomer with apparent molecular mass of about 240 kDa, A polyclonal a nti-peptide antiserum was raised against a synthetic 15-mer internal o ligopeptide sequence derived from the 75-kDa protein, The antiserum re cognized the purified binding protein in immunoblotting experiments an d precipitated the affinity-labeled protein from a crude extract of th e membrane fraction.