Publication Date:
1978-07-28
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kahane, I -- Gitler, C -- New York, N.Y. -- Science. 1978 Jul 28;201(4353):351-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663661" target="_blank"〉PubMed〈/a〉
Keywords:
Azides
;
Erythrocyte Membrane/*ultrastructure
;
Erythrocytes/*ultrastructure
;
*Glycophorin
;
Humans
;
Iodine Radioisotopes
;
Isotope Labeling
;
Membrane Lipids/blood
;
*Membrane Proteins/blood
;
Peptide Fragments
;
*Sialoglycoproteins
;
Solubility
;
Trypsin
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
