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.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 23 December 1966:
Vol. 154. no. 3756, pp. 1561 - 1562
DOI: 10.1126/science.154.3756.1561
Prev | Table of Contents | Next

Articles

Evolution of Immunoglobulin Polypeptide Chains: Carboxy-Terminal of an IgM Heavy Chain

Russell F. Doolittle 1, S. J. Singer 1, and Henry Metzger 2

1 Departments of Chemistry and Biology, University of California at San Diego, La Jolla
2 National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland

The dipeptide sequence at the carboxy-terminal of a heavy (µ) chain from a human macroglobulin ( IgM) is tyrosylcysteine, although the reverse sequence, cysteinyltyrosine, has not been rigorously excluded. The presence of cysteine at the carboxy-terminal was predicted from a recognition of the chemical homologies among the polypeptide chains of immunoglobulins, and their probable evolutionary origin.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Carboxy-Terminal Amino Acids of gammaA and gammaM Heavy Chains.
C. A. Abel and H. M. Grey (1967)
Science 156, 1609-1610
   Abstract »    PDF »
On the Structure of Antibody Active Sites.
S. J. Singer, L. I. Slobin, N. O. Thorpe, and J. W. Fenton II (1967)
Cold Spring Harb Symp Quant Biol 32, 99-110
   Abstract »    PDF »


To Advertise     Find Products

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