Distribution of Transmembrane Polypeptides in Freeze Fracture

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...

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Bibliographic Details
Published inScience (American Association for the Advancement of Science) Vol. 203; no. 4387; pp. 1343 - 1346
Main Authors Edwards, Harold H., Mueller, Thomas J., Morrison, Martin
Format Journal Article
LanguageEnglish
Published United States American Association for the Advancement of Science 30.03.1979
Subjects
Cell membranes
Erythrocyte membrane
Erythrocyte Membrane - ultrastructure
Erythrocytes
Erythrocytes - ultrastructure
Freeze Fracturing - methods
Gels
Glycoproteins - blood
Hemoglobins
Humans
Macromolecular Substances
Membrane proteins
Membrane Proteins - blood
Molecular Weight
P branes
Polylysine
Protein Binding
Protein Conformation
Sialoglycoproteins
Sodium
String theory
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Summary: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.
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ISSN:0036-8075
1095-9203
DOI:10.1126/science.424755