Publication Date:
1979-03-30
Description:
Human erythrocytes have been freeze-fractured, and the polypeptides associated with the separate halves of the membrane bilayer have been analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The transmembrane proteins were differentially separated by the fracture process. Although sialoglycoproteins associated with the outer half of the membrane, the anion transport protein (band 3) mainly remained with the inner half of the membrane. Well-defined fragments of the sialoglycoproteins were produced by the freeze-fracture procedure, indicating that selected covalent bonds of these transmembrane proteins were broken.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edwards, H H -- Mueller, T J -- Morrison, M -- New York, N.Y. -- Science. 1979 Mar 30;203(4387):1343-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/424755" target="_blank"〉PubMed〈/a〉
Keywords:
Erythrocyte Membrane/*ultrastructure
;
Erythrocytes/*ultrastructure
;
Freeze Fracturing/methods
;
Glycoproteins/blood
;
Humans
;
Macromolecular Substances
;
*Membrane Proteins/blood
;
Molecular Weight
;
Polylysine
;
Protein Binding
;
Protein Conformation
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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