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) 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.
D000199:Actins / Q000032:analysis; D001798:Blood Proteins / Q000032:analysis; D002463:Cell Membrane Permeability; D004548:Elasticity; D004910:Erythrocyte Membrane / Q000502:physiology / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis; D011487:Protein Conformation; D013049:Spectrin / Q000032:analysis; D013500:Surface Tension
D000199:Actins; D001798:Blood Proteins; D008565:Membrane Proteins; D013049:Spectrin