Binding studies on anti-fructofuranan mouse myeloma immunoglobulins A47N, A4, U61, and E109.
Four murine myeloma immunoglobulins, A4, A47N, U61, and E109, have been studied for their binding affinities with inulin and a series of oligosaccharides derived from inulin. The results indicate that the combining site of these immunoglobulins shows highest complementarity for a trifructofuranosyl sequence ( A4 and A47N) and a tetrafructofuranosyl sequence ( U61 and E109). The size of the combining area of the immunoglobulin E109 derived from the antigenic determinant (approximately 15 X 14 X 10 A) agrees well with the size observed on a hypothetical space model of the Fv portion of E109 (Potter, M., Rudikoff, S., Padlan, E. A., and Vrana, M. (1976), Antibodies in Human Diagnosis and Therapy, Haber, E., and Krause, R.M., Ed., New York, N.Y., Raven Press).[1]References
- Binding studies on anti-fructofuranan mouse myeloma immunoglobulins A47N, A4, U61, and E109. Streefkerk, D.G., Glaudemans, C.P. Biochemistry (1977) [Pubmed]
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