Erythrocyte membrane proteins: a modified Gorter-Grendel experiment

The pressure-area isotherm and shear resistance of spectrin-actin monolayers indicate a close-packed structure at about 1.0 m2/mg protein. This surface area is equivalent to a thickness of about two monolayers at the erythrocyte membrane inner face. The maximum elasticity (lowest compressibility) oc...

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Bibliographic Details
Published in:The Journal of membrane biology 1979-06, Vol.47 (2), p.185-193
Main Authors: Blank, M, Soo, L, Abbott, R E
Format: Article
Language:English
Subjects:
Actins - analysis
Blood Proteins - analysis
Cell Membrane Permeability
Elasticity
Erythrocyte Membrane - physiology
Erythrocyte Membrane - ultrastructure
Erythrocytes - ultrastructure
Humans
Membrane Proteins - analysis
Protein Conformation
Spectrin - analysis
Surface Tension
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Summary:The pressure-area isotherm and shear resistance of spectrin-actin monolayers indicate a close-packed structure at about 1.0 m2/mg protein. This surface area is equivalent to a thickness of about two monolayers at the erythrocyte membrane inner face. The maximum elasticity (lowest compressibility) occurs at 0.7 mg2/mg protein, indicating the limit of reversible compression. The mechanical properties of the monolayers approximate those of the intact membrane, suggesting that the structures are similar and that these monolayers may account for many of the in vivo properties.
ISSN:0022-2631
1432-1424
DOI:10.1007/BF01876116