Carbon-13 nuclear magnetic resonance study of the binding of carbon-13-enriched tetra-L-alanine haptens to Fab' fragments of anti-poly(L-alanine) antibodies

Geller, Shamir; Wei, Shen; Shkuda, G. K.; Marcus, Donald M.; Brewer, C. Fred

doi:10.1021/bi00556a030

Cited by 6 publications

(2 citation statements)

References 33 publications

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“…In previous n.m.r. studies the antigen has been a small peptide (Geller et al, 1980) or an isolated hapten (Dwek et al, 1977;Dower & Dwek, 1979). MBP is an antigen in which the epitope is a sequential region of amino acid residues.…”

Section: Discussionmentioning

confidence: 99%

Proton-n.m.r. study of interaction of myelin basic protein with a monoclonal antibody

Mendz¹,

Moore²,

Easterbrook‐Smith³

et al. 1985

Biochemical Journal

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Proton n.m.r. at 400 MHz has been applied to study the interactions of bovine or porcine myelin basic protein (b- or p-MBP) with a monoclonal antibody to human (h-) MBP. The antibody, an IgG immunoglobulin that contains a sequential epitopic region, cross-reacts with b-MBP but not with p-MBP, the presumed epitope being identical in h- and b-MBP. N.m.r. spectra were recorded from the Fab fragment of the antibody and for mixtures of Fab and MBP at various molar ratios. The n.m.r. spectrum of MBP in the mixture consists mostly of well resolved peaks against a broad background due to the Fab. With b-MBP, but not p-MBP, specific interactions are observed at the residue tyrosine-135, which is part of the epitopic sequence. Other interactions occur between the Fab and both b- and p-MBP at residues distant from the epitopic region. Standard radioassay techniques were employed to calculate the binding constants of both basic proteins with the immunoglobulin. The binding constant, Kb, for IgG to column-immobilized b-MBP at 298K is (0.95 +/- 0.07) X 10(7) dm3/mol. The value of Kb decreases with the ionic strength of the medium, suggesting a coulombic interaction between antigen and antibody. N.m.r. spectra were also measured for mixtures of the Fab fragment and peptides containing the epitopic site, with results in agreement with those for the whole protein.

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Section: Discussionmentioning

confidence: 99%

Proton-n.m.r. study of interaction of myelin basic protein with a monoclonal antibody

Mendz¹,

Moore²,

Easterbrook‐Smith³

et al. 1985

Biochemical Journal

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show abstract

“…Previous NMR studies on antibodies have concentrated on myeloma proteins with specificity for nitroaromatics (Dwek et al, 1977;Morris et al, 1980;Dower et al, 1978) and phosphorylcholine (Gettins et al, 1977;Goetze & Richards, 1977). More recently these methods have been applied to a 13C NMR study of a heterogeneous antibody population raised against polyalanine (Geller et al, 1980), though the heterogeneity limited the usefulness of the observations. Diversity, however, is the essence of the immune response, and it is therefore important to be able to compare different types of combining sites.…”

mentioning

confidence: 99%

Interaction of saccharide haptens with myeloma proteins. A 270-MHz proton NMR study

Gettins¹,

Boyd²,

Glaudemans³

et al. 1981

Biochemistry

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NMR Studies of Amino Acids, Peptides, and Proteins: A Brief Review, 1980-1982

Rattle¹

1985

Annual Reports on NMR Spectroscopy

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Carbon-13 nuclear magnetic resonance study of the binding of carbon-13-enriched tetra-L-alanine haptens to Fab' fragments of anti-poly(L-alanine) antibodies

Cited by 6 publications

References 33 publications

Proton-n.m.r. study of interaction of myelin basic protein with a monoclonal antibody

Proton-n.m.r. study of interaction of myelin basic protein with a monoclonal antibody

Interaction of saccharide haptens with myeloma proteins. A 270-MHz proton NMR study

NMR Studies of Amino Acids, Peptides, and Proteins: A Brief Review, 1980-1982

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