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. 1988 Apr;63(4):563–567.

Studies of a human lambda-chain epitope related to a complementarity-determining region.

H S Kim 1, H F Deutsch 1
PMCID: PMC1454789  PMID: 2452787

Abstract

A tryptic non-adecapeptide representing the 24-42 sequence of the MCG lambda-type Bence-Jones protein, and which contains its entire complementarity-determining region-1, was isolated. The peptide was utilized in preparing an affinity column that was used to isolate an antibody having the reactivity of a previously employed idiotypic antibody to MCG. This antibody preparation, as well as 13 monoclonal mouse antibodies to human lambda-chains, was employed in an enzyme-linked immunoassay to detect other Bence-Jones proteins with this serologic specificity. The results obtained with two of the monoclonal antibodies suggest that the epitope in question is a noncontiguous one.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Benjamin D. C., Berzofsky J. A., East I. J., Gurd F. R., Hannum C., Leach S. J., Margoliash E., Michael J. G., Miller A., Prager E. M. The antigenic structure of proteins: a reappraisal. Annu Rev Immunol. 1984;2:67–101. doi: 10.1146/annurev.iy.02.040184.000435. [DOI] [PubMed] [Google Scholar]
  2. Ely K. R., Wood M. K., Rajan S. S., Hodsdon J. M., Abola E. E., Deutsch H. F., Edmundson A. B. Unexpected similarities in the crystal structures of the Mcg light-chain dimer and its hybrid with the Weir protein. Mol Immunol. 1985 Feb;22(2):93–100. doi: 10.1016/s0161-5890(85)80002-x. [DOI] [PubMed] [Google Scholar]
  3. Fett J. W., Deutsch H. F. Primary structure of the Mcg lambda chain. Biochemistry. 1974 Sep 24;13(20):4102–4114. doi: 10.1021/bi00717a007. [DOI] [PubMed] [Google Scholar]
  4. Fett J. W., Deutsch H. F. The variability of human lambda-chain constant regions and some relationships to V-regions sequences. Immunochemistry. 1976 Feb;13(2):149–155. doi: 10.1016/0019-2791(76)90283-4. [DOI] [PubMed] [Google Scholar]
  5. Green N., Alexander H., Olson A., Alexander S., Shinnick T. M., Sutcliffe J. G., Lerner R. A. Immunogenic structure of the influenza virus hemagglutinin. Cell. 1982 Mar;28(3):477–487. doi: 10.1016/0092-8674(82)90202-1. [DOI] [PubMed] [Google Scholar]
  6. Jabusch J. R., Deutsch H. F. Primary structure of a human lambda-chain (Weir) of the Mcg type. Mol Immunol. 1982 Jul;19(7):901–906. doi: 10.1016/0161-5890(82)90356-x. [DOI] [PubMed] [Google Scholar]
  7. March S. C., Parikh I., Cuatrecasas P. A simplified method for cyanogen bromide activation of agarose for affinity chromatography. Anal Biochem. 1974 Jul;60(1):149–152. doi: 10.1016/0003-2697(74)90139-0. [DOI] [PubMed] [Google Scholar]
  8. McMillan S., Seiden M. V., Houghten R. A., Clevinger B., Davie J. M., Lerner R. A. Synthetic idiotypes: the third hypervariable region of murine anti-dextran antibodies. Cell. 1983 Dec;35(3 Pt 2):859–863. doi: 10.1016/0092-8674(83)90118-6. [DOI] [PubMed] [Google Scholar]
  9. Niman H. L., Houghten R. A., Walker L. E., Reisfeld R. A., Wilson I. A., Hogle J. M., Lerner R. A. Generation of protein-reactive antibodies by short peptides is an event of high frequency: implications for the structural basis of immune recognition. Proc Natl Acad Sci U S A. 1983 Aug;80(16):4949–4953. doi: 10.1073/pnas.80.16.4949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Schwartz W. E., Smith P. K., Royer G. P. N-(beta-Iodoethyl)trifluoroacetamide: a new reagent for the aminoethylation of thio groups in proteins. Anal Biochem. 1980 Jul 15;106(1):43–48. doi: 10.1016/0003-2697(80)90116-5. [DOI] [PubMed] [Google Scholar]
  11. Solomon A. Light chains of human immunoglobulins. Methods Enzymol. 1985;116:101–121. doi: 10.1016/s0076-6879(85)16008-8. [DOI] [PubMed] [Google Scholar]
  12. Tainer J. A., Getzoff E. D., Alexander H., Houghten R. A., Olson A. J., Lerner R. A., Hendrickson W. A. The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein. Nature. 1984 Nov 8;312(5990):127–134. doi: 10.1038/312127a0. [DOI] [PubMed] [Google Scholar]
  13. Walker M. R., Solomon A., Ling N. R., Brown B., Lowe J. A., Hardie D., Jefferis R. Immunogenic and antigenic epitopes of immunoglobulins. XVIII. Subpopulations of human lambda chains defined with a panel of monoclonal antibodies. Immunology. 1986 Nov;59(3):467–471. [PMC free article] [PubMed] [Google Scholar]
  14. Walker M., Hardie D., Lowe J., Ling N. R., De Lange G., Jefferis R. Immunogenicity and antigenicity of immunoglobulins. XII. Intact light chain and heavy chain isotype-restricted Vk-associated epitopes. Immunology. 1985 Jun;55(2):205–211. [PMC free article] [PubMed] [Google Scholar]
  15. Wilson I. A., Haft D. H., Getzoff E. D., Tainer J. A., Lerner R. A., Brenner S. Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition. Proc Natl Acad Sci U S A. 1985 Aug;82(16):5255–5259. doi: 10.1073/pnas.82.16.5255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Young D. R., Schmitz H. E., Atassi M. Z. Antibodies with specificities to preselected protein regions evoked by free synthetic peptides representing protein antigenic sites or other surface locations: demonstration with myoglobin. Mol Immunol. 1983 May;20(5):567–570. doi: 10.1016/0161-5890(83)90096-2. [DOI] [PubMed] [Google Scholar]
  17. Zhu D., Kim H. S., Deutsch H. F. Variable-region sequences of five human lambda-chain proteins reacting with an idiotypic antibody to the MCG Bence-Jones protein. Mol Immunol. 1983 Oct;20(10):1107–1116. doi: 10.1016/0161-5890(83)90120-7. [DOI] [PubMed] [Google Scholar]

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