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/lp/karger/recombination-experiments-with-an-unusual-l-chain-related-myeloma-0Yg5uShgfr
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- Publisher
- Karger
- Copyright
- © 1973 S. Karger AG, Basel
- ISSN
- 0001-5792
- eISSN
- 1421-9662
- DOI
- 10.1159/000208398
- Publisher site
- See Article on Publisher Site
Abstract
The occurrence of a light chain related myeloma protein, which was defective compared with complete light chains, gave rise to further investigation of its structure. Mixing of <sup>125</sup>I-labelled polypeptide chains resulting from the reduction of this protein with heavy and light polypeptide chains of an <sup>131</sup>I-labelled myeloma protein showed recombination to a considerable extent. Fragments of L-chains, as it appears from these experiments, may exist as dimers stabilized by noncovalent bonds. Their interaction with light and heavy chains in vivo might compete with the normal assembly of immunoglobulin polypeptide chains.
Journal
Acta Haematologica – Karger
Published: Jan 1, 2009
Keywords: Myeloma proteins; Polypeptide chain; Antibody formation; Immunoglobulin structure; Light chain fragments