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Immunochemical reactivity of soybean -conglycinin subunits

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The immunochemical reactivity of two polyclonal sera raised against soybean purified αα′ and  subunits was analysed. We show that anti-αα′ serum mainly reacts with αα′ subunits and ′ subunit, but it does not recognize  subunit. In addition,  subunit is not able to compete with αα′ subunit for anti-αα′ serum recognition sites; therefore the main immunogenic region of αα′ subunits is the extension region. Both anti-αα′ and anti- sera were able to recognize E. coli produced α subunit, consequently glycosylation is apparently not required for antigen–antibody interaction. Anti- subunit serum shows strong reactivity against soybean produced -subunit and recombinant α subunit, while it shows weak recognition of soybean purified αα′ subunits. A mutant of α subunit with the N terminal  barrel region and C terminal α helices deleted, failed to be recognized by anti- serum. For that reason although N and C terminal domains are structurally equivalent, their immunochemical reactivity is different.
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Keywords: immunoreactivity; recombinant soybean subunits; soybean 7S globulin; -conglycinin

Document Type: Research Article

Affiliations: Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Capital Federal, Argentina

Publication date: March 1, 2005

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