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Isolation of a French bean (Phaseolus vulgaris L.) homolog to the β-glucan elicitor-binding protein of soybean (Glycine max L.)

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Mithöfer, A., Fliegmann, J., & Ebel, J. (1999). Isolation of a French bean (Phaseolus vulgaris L.) homolog to the β-glucan elicitor-binding protein of soybean (Glycine max L.). Biochimica et Biophysica Acta-Biomembranes, 1418(1), 127-132. doi:10.1016/s0005-2736(99)00010-3.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-4CF6-F
Abstract
A high-affinity membrane-bound β-glucan elicitor-binding protein has been purified from microsomal preparations of French bean (Phaseolus vulgaris L.) roots. A 5900-fold purification was achieved by affinity chromatography of functionally solubilized membrane proteins. The β-glucan-binding protein had an apparent molecular mass of 78 kDa when subjected to SDS-PAGE. Western blot analysis showed specific crossreactivity of this French bean protein with an antiserum raised against a synthetic peptide representing an internal 15 amino acid fragment of the β-glucan-binding protein from soybean. Northern blot analysis with a cDNA probe of the soybean β-glucan-binding protein gene revealed a crosshybridizing transcript of 2.4 kb in French bean. These results indicate that the β-glucan-binding proteins of French bean and soybean are conserved homologs involved in β-glucan elicitor recognition.