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Carbohydrate binding activity of a lectin-like glycoprotein from stems and leaves of Dolichosbiflorus
Authors:Marilynn E. Etzler  Carl Borrebaeck
Affiliation:Department of Biochemistry and Biophysics University of California Davis, California 95616 USA
Abstract:A glycoprotein from the stems and leaves of the Dolichosbiflorus plant that cross reacts with antibodies to the seed lectin has been found to bind to affinity columns of blood group A + H substance covalently linked to Sepharose. This binding of the cross reactive material to the affinity resin differs from that of the seed lectin in that it is easily dissociated with 0.15 M NaCl. Affinity electrophoresis using entrapped blood group A + H substance shows that the carbohydrate binding activity of the cross reactive material is weakly inhibited with N-acetyl-D
/></figure>-galactosamine and N-acetyl-D<figure class=/></figure>-glucosamine. Glucose, mannose and galactose gave no inhibition when tested at concentrations of 50 mM. These data indicate that the specificity of the cross reactive material is somewhat different from the N-acetyl-D<figure class=/></figure>-galactosamine specificity of the seed lectin. The significance of these findings is discussed in relation to the structural similarities of the cross reactive material and the seed lectin.</td>
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Keywords:CRM  cross reactive material to antibodies against the seed lectin  SDS  sodium dodecyl sulfate  PBS  PEG  polyethylene glycol  BGS  blood group A + H substance
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