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Anti-Idiotypes, Receptors, and Molecular Mimicry by D. Scott Linthicum, Nadir R. Farid

By D. Scott Linthicum, Nadir R. Farid

Here is an updated evaluation of vital new tools and ends up in anti-idiotypes, receptors, and molecular mimicry.It starts with a dialogue of the theoretical history ofthe anti-idiotypic community, it truly is position within the law of immune reaction, and the actual features of anti-idiotypic antibodies. It then is going directly to discover many exciting functions in such parts as insulin motion, thyroid telephone functionality, the neurosciences, cardiology, virology, pharmacology, and replica.

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The negatively charged side chain of aspartic acid is appropriate for interactions with the positively charged rhodamine ligand. Finally, the positioning of aspartic acid 97 in the third hypervariable loop places its side chain in a region which is very accessible for external interactions. 9 idiotope. Of particular interest is the finding that the idiotope is significantly altered by conformational effects accompanying the binding of ligand in a site remote from the idiotypic determinant. This observation should be considered in arguments concerning mimicry of antigen by anti-idiotype.

For each compound, the cross-reactivity was compared with the biological activities (the hypotensive effect in the rat in vivo and the spasmogenic action on the guinea pig ileum in vitro) to get an idea about the expected resemblance between anti-SP Abs and the SP receptor. 2, there is a good correlation between the three parameters (cross-reactivity and the two selected biological activities). , the C-terminal pentapeptide, especially Phe 7 , Phe 8 , Leu lll , and Mee l NH 2 ) and hence strongly suggest that the paratopes of anti-SP Abs and SP receptor binding sites carry similar structural features.

Chain sequence. Of the nine residues which form the outer rim of the binding cavity of the dimer, aspartic acid 97 is the only residue contributed exclusively by monomer 2. This residue is not found in a comparable location in monomer I and is not present in the sequences of ViI and Weir, which fail to express the idiotope. The negatively charged side chain of aspartic acid is appropriate for interactions with the positively charged rhodamine ligand. Finally, the positioning of aspartic acid 97 in the third hypervariable loop places its side chain in a region which is very accessible for external interactions.

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