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1.
J Immunol ; 122(2): 537-41, 1979 Feb.
Article in English | MEDLINE | ID: mdl-105048

ABSTRACT

Five murine myeloma immunoglobulins have been studied for their binding with fructose-containing homopolysaccharides. The results indicate that the anti-(2 leads to 1)-D-fructofuranans are capable of binding (2 leads to 6)-D-fructofuranans with reduced affinity. An anti-(2 leads to 6)-D-fructofuranan (U10) was incapable of binding a (2 leads to 1)-D-fructofuranan. By using molecular models of fructofuranans of both linkage types, and a hypothetical molecular model of the combining region of E109, an anti-(2 leads to 1)-D-fructofuranan, a rationalization of these date can be proposed.


Subject(s)
Antibody Specificity , Binding Sites, Antibody , Immunoglobulin Fab Fragments/immunology , Inulin/immunology , Myeloma Proteins/immunology , Animals , Fluorescent Antibody Technique , Fructans/immunology , Immunodiffusion , Mice , Mice, Inbred BALB C
3.
J Immunol ; 120(2): 408-10, 1978 Feb.
Article in English | MEDLINE | ID: mdl-413866

ABSTRACT

Heterologous H-L chain recombinants derived from homogeneous murine myeloma immunoglobulins with anti-inulin specificity were found to bind inulin-related oligosaccharides with affinities closely paralleling those of the L chain donors.


Subject(s)
Antibody Specificity , Fructans , Immunoglobulin A , Polysaccharides , Animals , Binding Sites, Antibody , Immunoglobulin A/chemical synthesis , Immunoglobulin Heavy Chains , Immunoglobulin Light Chains , Inulin , Mice , Myeloma Proteins
4.
Biochemistry ; 16(17): 3760-5, 1977 Aug 23.
Article in English | MEDLINE | ID: mdl-901750

ABSTRACT

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).


Subject(s)
Carbohydrates/immunology , Immunoglobulin A , Immunoglobulin Fab Fragments , Myeloma Proteins , Animals , Binding Sites, Antibody , Fructose/immunology , Inulin/immunology , Ligands , Mice , Models, Molecular , Molecular Conformation , Plasmacytoma/immunology , Precipitin Tests , Spectrometry, Fluorescence
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