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.
GoGreen Membership

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 15 October 1965:
Vol. 150. no. 3694, pp. 361 - 363
DOI: 10.1126/science.150.3694.361
Prev | Table of Contents | Next

Articles

Macroglobulin-Producing Plasma-Cell Tumor in Mice: Identification of a New Light Chain

K. R. Mcintimif 1, R. M. Asofsky 1, M. Potter 1, and E. L. Kuff 1

1 National Cancer Institute and National Institute of Allergy and Infectious, Disease. Bethesda, Maryland 20014

A transplantable plasmacell tumor in mice produces both a ggrM-macroglobulin serum protein with a sedimentation coefficient of 17S and a kappa-type urinary protein. The reduced and alkylated macroglobulin, when examined by electrophoresis in acid-urea polyacrylamide gel, had a fast component which migrated in the same position as the urinary protein and also a slow component. These two components, as shown by exclusion chromatography, represent the light and heavy polypeptide chains of the ggrM-macroglobulin. The aforementioned macroglobulin was antigenically related to that in normal mouse serum.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Two Types Of Lambda Polypeptide Chains In Human Immunoglobulins.
D. Ein and J. L. Fahey (1967)
Science 156, 947-948
   Abstract »    PDF »
Light Chains of Mouse Myeloma Proteins: Partial Amino Acid Sequence.
R. Perham, E. Appella, and M. Potter (1966)
Science 154, 391-393
   Abstract »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

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