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 28 July 1978:
Vol. 201. no. 4353, pp. 351 - 352
DOI: 10.1126/science.663661

Articles

Science, Vol 201, Issue 4353, 351-352
Copyright © 1978 by American Association for the Advancement of Science


articles

Red cell membrane glycophorin labeling from within the lipid bilayer

I Kahane and C Gitler

Human red blood cell membranes were labeled from within the lipid bilayer by the apolar photosensitive reagent, 5-[125I]iodonaphthyl-1-azide. Glycophorin, the major sialoglycoprotein of the red cell membrane, was purified by two different methods; it contained approximately half of the total label incorporated into membrane proteins. The label was confined to the trypsin-insoluble peptide of glycophorin that includes a sequence of 20, mainly apolar, amino acids. These findings provide direct evidence that the labeled segment resides within the membrane in direct contact with the lipid bilayer, and support the suggestion that glycophorin spans the bilayer through its hydrophobic domain.





To Advertise     Find Products


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