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 18 October 1968:
Vol. 162. no. 3851, pp. 365 - 367
DOI: 10.1126/science.162.3851.365
Prev | Table of Contents | Next

Articles

Conformation of Blood-Group and Virus Receptor Glycoproteins from Red Cells and Secretions

Bruno Jirgensons 1 and Georg F. Springer 2

1 Department of Biochemistry, University of Texas, M. D. Anderson Hospital and Tumor Institute, Houston 77025
2 Department of Immunochemistry Research, Evanston Hospital, Northwestern University, Evanston, Illinois 60201

Optical rotatory dispersion of human blood-group and virus receptor glycoproteins from erythrocytes and secretions was studied in the far-ultraviolet. Erythrocyte membrane blood-group glycoproteins, with potent virus receptor activities, contained significant alpha-helical and extended beta conformations, whereas the glycoproteins of secretions were largely disordered. These conclusions were supported by determination of the Moffitt constants (b0) and by measurements of circular dichroism.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
T and Tn, general carcinoma autoantigens.
G. Springer (1984)
Science 224, 1198-1206
   Abstract »    PDF »


To Advertise     Find Products

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