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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1975 Jul;72(7):2511–2514. doi: 10.1073/pnas.72.7.2511

Region of immunoglobulin light-chain mRNA transcribed into complementary DNA by RNA-dependent DNA polymerase of avian myeloblastosis virus.

I Schechter
PMCID: PMC432798  PMID: 52155

Abstract

The mRNA coding for a kappa-type immunoglobulin light (L)-chain and its complementary DNA (cDNA) hybridize with a Crt1/2 of 2.6 x 10(-4) moles of ribonucleotide x liter-1 x sec, forming well-matched duplexes (melting temperature Tm equals 89 degrees). The molecular weight of the cDNA is about 280,000 (840 nucleotides) as determined by alkaline sucrose gradient centrifugation and from the extent of protection of the mRNA by the cDNA from ribonuclease digestion. The cDNA anneals with kappa-type mRNAs of the same and different subgroups with comparable Crt1/2 values, but not with a lambda-type mRNA. Thus, one kappa-type cDNA can be used to quantify the mRNAs coding for all kappa-type L-chains. The values of cDNA hybridized at saturation with various kappa-type mRNAs indicate that: (1) the cDNA is complementary to the entire constant region and to about half of the variable (V)-region; (2) V-regions of similar amino-acid sequence are coded by a similar nucleotide sequence; (3) the nucleic acid probe to one V-region may anneal and quantify V-region genes of members of the same subgroup.

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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. Brownlee G. G., Cartwright E. M., Cowan N. J., Jarvis J. M., Milstein C. Purification and sequence of messenger RNA for immunoglobulin light chains. Nat New Biol. 1973 Aug 22;244(138):236–240. doi: 10.1038/newbio244236a0. [DOI] [PubMed] [Google Scholar]
  3. Faust C. H., Diggelmann H., Mach B. Estimation of the number of genes coding for the constant part of the mouse immunoglobulin kappa light chain. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2491–2495. doi: 10.1073/pnas.71.6.2491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fudenberg H. H., Wang A. C., Pink J. R., Levin A. S. Studies of an unusual biclonal gammopathy: implications with regard to genetic control of normal immunoglobulin synthesis. Ann N Y Acad Sci. 1971 Dec 31;190:501–506. doi: 10.1111/j.1749-6632.1971.tb13559.x. [DOI] [PubMed] [Google Scholar]
  5. Honjo T., Packman S., Swan D., Nau M., Leder P. Organization of immunoglobulin genes: reiteration frequency of the mouse kappa chain constant region gene. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3659–3663. doi: 10.1073/pnas.71.9.3659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kacian D. L., Spiegelman S. Use of micrococcal nuclease to monitor hybridization reactions with DNA. Anal Biochem. 1974 Apr;58(2):534–540. doi: 10.1016/0003-2697(74)90221-8. [DOI] [PubMed] [Google Scholar]
  7. McKean D., Potter M., Hood L. Mouse immunoglobulin chains. Pattern of sequence variation among kappa chains with limited sequence differences. Biochemistry. 1973 Feb;12(4):760–771. doi: 10.1021/bi00728a028. [DOI] [PubMed] [Google Scholar]
  8. Ruprecht R. M., Goodman N. C., Spiegelman S. Determination of natural host taxonomy of RNA tumor viruses by molecular hybridization: application to RD-114, a candidate human virus. Proc Natl Acad Sci U S A. 1973 May;70(5):1437–1441. doi: 10.1073/pnas.70.5.1437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. STUDIER F. W. SEDIMENTATION STUDIES OF THE SIZE AND SHAPE OF DNA. J Mol Biol. 1965 Feb;11:373–390. doi: 10.1016/s0022-2836(65)80064-x. [DOI] [PubMed] [Google Scholar]
  10. Schechter I. Aggregates of partially purified mRNA coding for immunoglobulin light-chain. Biochem Biophys Res Commun. 1974 Apr 8;57(3):857–864. doi: 10.1016/0006-291x(74)90625-1. [DOI] [PubMed] [Google Scholar]
  11. Schechter I. Biologically and chemically pure mRNA coding for a mouse immunoglobulin L-chain prepared with the aid of antibodies and immobilized oligothymidine. Proc Natl Acad Sci U S A. 1973 Aug;70(8):2256–2260. doi: 10.1073/pnas.70.8.2256. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Schechter I. Partial amino acid sequence of the precursor of immunoglobulin light chain programmed by messenger RNA in vitro. Science. 1975 Apr 11;188(4184):160–162. doi: 10.1126/science.803715. [DOI] [PubMed] [Google Scholar]
  13. Schechter I. Use of antibodies for the isolation of biologically pure messenger ribonucleic acid from fully functional eukaryotic cells. Biochemistry. 1974 Apr 23;13(9):1875–1885. doi: 10.1021/bi00706a016. [DOI] [PubMed] [Google Scholar]
  14. Scherberg N. H., Refetoff S. The radioiodination of ribopolymers for use in hybridizational and molecular analyses. J Biol Chem. 1974 Apr 10;249(7):2143–2150. [PubMed] [Google Scholar]
  15. Smith G. P., Hood L., Fitch W. M. Antibody diversity. Annu Rev Biochem. 1971;40:969–1012. doi: 10.1146/annurev.bi.40.070171.004541. [DOI] [PubMed] [Google Scholar]
  16. Staynov D. Z., Pinder J. C., Gratzer W. B. Molecular weight determination of nucleic acids by gel electrophoresis in non-aqueous solution. Nat New Biol. 1972 Jan 26;235(56):108–110. doi: 10.1038/newbio235108a0. [DOI] [PubMed] [Google Scholar]
  17. Sutton W. D., McCallum M. Mismatching and the reassociation rate of mouse satellite DNA. Nat New Biol. 1971 Jul 21;232(29):83–85. doi: 10.1038/newbio232083a0. [DOI] [PubMed] [Google Scholar]
  18. Tonegawa S., Bernardini A., Weimann B. J., Steinberg C. Reiteration frequency of antibody genes. Studies with k-chain mRNA. FEBS Lett. 1974 Mar 15;40(1):92–96. doi: 10.1016/0014-5793(74)80901-4. [DOI] [PubMed] [Google Scholar]
  19. Wetmur J. G., Davidson N. Kinetics of renaturation of DNA. J Mol Biol. 1968 Feb 14;31(3):349–370. doi: 10.1016/0022-2836(68)90414-2. [DOI] [PubMed] [Google Scholar]

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