These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Recombination of heavy and light chains of human gamma-a-myeloma proteins: formation of hybrid molecules and configurational specificity.
    Author: Prendergast RA, Grey HM, Kunkel HG.
    Journal: J Exp Med; 1966 Aug 01; 124(2):185-97. PubMed ID: 4162153.
    Abstract:
    The present studies demonstrate that the conditions necessary for reductive cleavage, isolation, and recombination of L and H polypeptide chains of human gammaA-myeloma globulins parallel those required for similar manipulation of the component chains of gammaG-globulin. Specificity of recombination was shown for chains derived from the same protein. In contrast, no intradass preferential recombination was demonstrable. Hybrid molecules, formed by reassociation of noncovalent bonds, could be synthesized from isolated chains of two immunoglobulin classes resulting in the formation of molecules of the type gammaA-H-gammaG-L and gammaG-H-gammaA-L. Several sera containing both gammaA- and gammaG-"monoclonal" peaks were studied, one of which demonstrated the L chains associated with both peaks to be identical both by electrophoretic mobility in acid-urea gel and antigenic analysis. The possibility is considered that this case represents a naturally occurring analogue of the artificially produced hybrid molecules described in this study. Configurational antigenic specificity of gammaA-myeloma proteins, imposed by the presence of kappa L chains in native and appropriately recombined molecules, provides a further indication of the importance of noncovalent bonds in the establishment of the quaternary structure of these proteins.
    [Abstract] [Full Text] [Related] [New Search]