One-step purification of the beta-glucan elicitor-binding protein from soybean 
(Glycine max L.) roots and characterization of an anti-peptide antiserum

Mithöfer, Axel; Lottspeich, F.; Ebel, J.

doi:10.1016/0014-5793(96)00126-3

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One-step purification of the beta-glucan elicitor-binding protein from soybean (Glycine max L.) roots and characterization of an anti-peptide antiserum

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http://dx.doi.org/10.1016/0014-5793(96)00126-3
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Mithöfer, A., Lottspeich, F., & Ebel, J. (1996). One-step purification of the beta-glucan elicitor-binding protein from soybean (Glycine max L.) roots and characterization of an anti-peptide antiserum. FEBS Letters, 381(3), 203-207. doi:10.1016/0014-5793(96)00126-3.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-4D17-8

Abstract

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 preparation consisted of one major protein with an apparent molecular mass of about 75 kDa, Electrophoretic analyses of the purified and photoaffinity-labeled binding protein showed that the native protein was an oligomer with apparent molecular mass of about 240 kDa, A polyclonal anti-peptide antiserum was raised against a synthetic 15-mer internal oligopeptide sequence derived from the 75-kDa protein, The antiserum recognized the purified binding protein in immunoblotting experiments and precipitated the affinity-labeled protein from a crude extract of the membrane fraction.