Read e-book online Anti-Idiotypes, Receptors, and Molecular Mimicry PDF

By D. Scott Linthicum, Nadir R. Farid

ISBN-10: 1461237343

ISBN-13: 9781461237341

ISBN-10: 1461283256

ISBN-13: 9781461283256

Here is an up to date evaluation of significant new equipment and ends up in anti-idiotypes, receptors, and molecular mimicry.It starts with a dialogue of the theoretical heritage ofthe anti-idiotypic community, it is function within the legislation of immune reaction, and the actual features of anti-idiotypic antibodies. It then is going directly to discover many exciting functions in such components as insulin motion, thyroid telephone functionality, the neurosciences, cardiology, virology, pharmacology, and replica.

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Extra resources for Anti-Idiotypes, Receptors, and Molecular Mimicry

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L.. M. Smith. E. Blalock. 1985. Similarity between the corticotropin (ACTH) receptor and a peptide encoded by an RNA that is complementary to ACTH mRNA. Proc. Natl. Acad. Sci. USA 82:1372. 5. Bost. K. E. Blalock. 1985. Molecular characterization of a corticotropin (ACTH) receptor. Mol. Cell. Endocrinol. 44: I. 6. Payet. O .. and E. Escher. 1985. ACTH receptors in rat adrenal glomerulosa cells. Endocrinology 117:38. 44 Kenneth L. Bost. Lawrence R. Smith. and J. Edwin Blalock 7. McIlhinney. J .. and D.

Thus, the peptide specified by the complementary RNA for LHRH mRNA is similar, if not identical, to the LHRH binding site since the peptide bound LHRH and the anti-peptide antibody bound the LHRH receptor. Binding Sites Encoded by Complementary Segments of Nucleic Acids From the three examples given above, it is quite clear that peptides encoded by complementary RNAs represent binding sites for the respective ligands. These findings, however, raise a question as to the relationship between ligands, their binding sites, and the genomic DNA from which they are ultimately translated.

9 Monoclonal Anti-Idiotype Three cloned cell lines exhibiting putative anti-Mcg idiotype specificity were obtained from two fusions using splenocytes from mice immunized with the Mcg protein. 9 was further characterized and used exclusively in this study. 1. The antibody reacted only with the immunizing Mcg L chain dimer and with no other Ig or Ig polypeptide chain. 9 was shown to bind to Mcg IgG in addition to the Mcg dimer (Fig. 2). 9 to solid-phase-adsorbed Mcg dimer, I J-LM Mcg dimer (50J-Lg/ml) was required to achieve an equivalent level of inhibition.

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

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