Skip to main content
NCBI home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1978 Nov 1;148(5):1388–1399. doi: 10.1084/jem.148.5.1388

The natural abundance of lambda2-light chains in inbred mice

PMCID: PMC2185043  PMID: 102727

Abstract

The amino acid sequence of the constant (C) domain of the light chain of the mouse myeloma protein M315 has not been identified so far in any other myeloma protein. In this study, serological analysis with antiserum to the C-domain of this light chain (L315) showed that approximately equal to 1% of Igs in normal mouse serum have L chains of the L315 type (called lambda2). Corroborative evidence was obtained by analysis of the carboxyterminal amino acid removed from normal light chains by carboxypeptidase A. A survey of 35 inbred mouse strains showed that all had lambda2; the serum level of Igs with lambda2-chains ranged from approximately equal to 140 microgram/ml in AL/N mice to approximately equal to 25 microgram/ml in SJL, BSVS, and eight other strains. In accord with the anti-Dnp activity of M315, sera from mice immunized with Dnp-KLH had three- to fivefold more lambda2 than sera from control mice immunized with KLH. It was also possible to measure serum immunoglobulin molecules bearing the lambda2 variable region of M315 (VL315). In BALB/c sera, the concentration of VL315 was about sixfold lower than that measured for lambda2. Thus, lambda2-chains are divided into at least two subsets: those whose V domain is indistinguishable from VL315 and those whose VL differs from VL315. A 10-fold increase in VL315 was obtained by immunizing BALB/c mice with Dnp-KLH. The relationship of the VL domains of normal immunoglobulin lambda2-chains to the embryonic Vlambda gene recently sequenced by Tonegawa et al., is discussed.

Full Text

The Full Text of this article is available as a PDF (703.7 KB).

Selected References

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

  1. Appella E. Amino acid sequences of two mouse immunoglobulin lambda chains. Proc Natl Acad Sci U S A. 1971 Mar;68(3):590–594. doi: 10.1073/pnas.68.3.590. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Biozzi G., Asofsky R., Lieberman R., Stiffel C., Mouton D., Benacerraf B. Serum concentrations and allotypes of immunoglobulins in two lines of mice genetically selected for "high" or "low" antibody synthesis. J Exp Med. 1970 Oct 1;132(4):752–764. doi: 10.1084/jem.132.4.752. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blaser K., Eisen H. N. Lambda2 light chains in normal mouse immunoglobulins. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1495–1499. doi: 10.1073/pnas.75.3.1495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blomberg B., Geckeler W. R., Weigert M. Genetics of the antibody response to dextran in mice. Science. 1972 Jul 14;177(4044):178–180. doi: 10.1126/science.177.4044.178. [DOI] [PubMed] [Google Scholar]
  5. Cesari I. M., Weigert M. Mouse lambda-chain sequences. Proc Natl Acad Sci U S A. 1973 Jul;70(7):2112–2116. doi: 10.1073/pnas.70.7.2112. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem. 1970 Jun;245(12):3059–3065. [PubMed] [Google Scholar]
  7. Dugan E. S., Bradshaw R. A., Simms E. S., Eisen H. N. Amino acid sequence of the light chain of a mouse myeloma protein (MOPC-315). Biochemistry. 1973 Dec 18;12(26):5400–5416. [PubMed] [Google Scholar]
  8. Eisen H. N., Simms E. S., Potter M. Mouse myeloma proteins with antihapten antibody acitivity. The protein produced by plasma cell tumor MOPC-315. Biochemistry. 1968 Nov;7(11):4126–4134. doi: 10.1021/bi00851a048. [DOI] [PubMed] [Google Scholar]
  9. Goetzl E. J., Metzger H. Affinity labeling of a mouse myeloma protein which binds nitrophenyl ligands. Kinetics of labeling and isolation of a labeled peptide. Biochemistry. 1970 Mar 3;9(5):1267–1278. doi: 10.1021/bi00807a031. [DOI] [PubMed] [Google Scholar]
  10. Hiramoto R., Ghanta V. K., McGhee J. R., Schrohenloher R., Hamlin N. M. Use of dextran conjugated columns for the isolation of large quantities of MOPC 104E IgM. Immunochemistry. 1972 Dec;9(12):1251–1253. doi: 10.1016/0019-2791(72)90300-x. [DOI] [PubMed] [Google Scholar]
  11. Inbar D., Hochman J., Givol D. Localization of antibody-combining sites within the variable portions of heavy and light chains. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2659–2662. doi: 10.1073/pnas.69.9.2659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Inbar D., Rotman M., Givol D. Crystallization with hapten of the Fab' fragment from a mouse IgA myeloma protein with antidinitrophenyl activity. J Biol Chem. 1971 Oct 25;246(20):6272–6275. [PubMed] [Google Scholar]
  13. KUNKEL H. G. Zone electrophoresis. Methods Biochem Anal. 1954;1:141–170. doi: 10.1002/9780470110171.ch6. [DOI] [PubMed] [Google Scholar]
  14. Potter M. Immunoglobulin-producing tumors and myeloma proteins of mice. Physiol Rev. 1972 Jul;52(3):631–719. doi: 10.1152/physrev.1972.52.3.631. [DOI] [PubMed] [Google Scholar]
  15. Sakato N., Eisen H. N. Antibodies to idiotypes of isologous immunoglobulins. J Exp Med. 1975 Jun 1;141(6):1411–1426. doi: 10.1084/jem.141.6.1411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schulenburg E. P., Simms E. S., Lynch R. G., Bradshaw R. A., Eisen H. N. Amino acid sequence of the light chain from a mouse myeloma protein with anti-hapten activity: evidence for a third type of light chain. Proc Natl Acad Sci U S A. 1971 Nov;68(11):2623–2626. doi: 10.1073/pnas.68.11.2623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Sonoda S., Schlamowitz M. Studies of 125I trace labeling of immunoglobulin G by chloramine-T. Immunochemistry. 1970 Nov;7(11):885–898. doi: 10.1016/0019-2791(70)90051-0. [DOI] [PubMed] [Google Scholar]
  18. Tonegawa S., Maxam A. M., Tizard R., Bernard O., Gilbert W. Sequence of a mouse germ-line gene for a variable region of an immunoglobulin light chain. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1485–1489. doi: 10.1073/pnas.75.3.1485. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tung A. S., Ju S. T., Sato S., Nisonoff A. Production of large amounts of antibodies in individual mice. J Immunol. 1976 Mar;116(3):676–681. [PubMed] [Google Scholar]
  20. Underdown B. J., Simms E. S., Eisen H. N. Subunit structure and number of combining sites of the immunoglobulin A myeloma protein produced by mouse plasmacytoma MOPC-315. Biochemistry. 1971 Nov 23;10(24):4359–4368. doi: 10.1021/bi00800a002. [DOI] [PubMed] [Google Scholar]
  21. Unkeless J. C., Eisen H. N. Binding of monomeric immunoglobulins to Fc receptors of mouse macrophages. J Exp Med. 1975 Dec 1;142(6):1520–1533. doi: 10.1084/jem.142.6.1520. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Wilde C. E., 3rd, Koshland M. E. Molecular size and shape of the J chain from polymeric immunoglobulins. Biochemistry. 1973 Aug 14;12(17):3218–3224. doi: 10.1021/bi00741a012. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES