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
Axel MithoferJ Ebel

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.

References

Jun 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·W E Schmidt, J Ebel

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Citations

Sep 2, 1998·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·J Ebel
Feb 12, 2004·Biochimica Et Biophysica Acta·William S YorkJocelyn K C Rose
Dec 18, 2013·Journal of Agricultural and Food Chemistry·Franco Gozzo, Franco Faoro
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Jan 1, 1998·Journal of Cellular Biochemistry·Marilynn E Etzler
Dec 20, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Nathalie GuarnizoMaría Bianney Bermúdez-Cardona

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