Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 21 October 1966:
Vol. 154. no. 3747, pp. 391 - 393
DOI: 10.1126/science.154.3747.391
Prev | Table of Contents | Next

Articles

Light Chains of Mouse Myeloma Proteins: Partial Amino Acid Sequence

Richard Perham 1, Ettore Appella 2, and Michael Potter 2

1 Department of Biochemistry, University of Cambridge, England; Department of Molecular Biophysics, Yale University, New Haven, Conn. 06520.
2 Laboratory of Biology, National Cancer Institute, Bethesda, Maryland

Five kappa chains in the urinary proteins of the BALB/c mouse have the same carboxyl terminal amino acid sequence; this sequence resembles that of kappa light chains in human immunoglobulins. The five chains have amino acid sequence variations at the amino- terminal. The genetic basis for the amino- terminal variations is not understood but could be due either to a mecha nism for differently translating a single genetic message or to the presence of more than one kappa- type structural cistron in the BALB/c genome.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Mechanism of Antibody Diversity: Germ Line Basis for Variability.
L. Hood and D. W. Talmage (1970)
Science 168, 325-334
   PDF »
The Structure of Immunoglobulin Light Chains.
E. Appella and R. N. Perham (1967)
Cold Spring Harb Symp Quant Biol 32, 37-44
   Abstract »    PDF »
Biosynthesis of the Carbohydrate Portion of Immunoglobulin Chains: Possible Relation to Secretion.
F. Melchers and P. M. Knopf (1967)
Cold Spring Harb Symp Quant Biol 32, 255-262
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)