pH-induced denaturation of spectrin changes the interaction of membrane proteins in erythrocyte ghosts. Biochemical and electron microscopic evidence.
The influence of different buffer pH values on the properties of spectrin in erythrocyte ghosts and on isolated spectrin was investigated. Ultrastructural findings and the results of biochemical studies show that denaturation and aggregation of spectrin molecules rather than disulfide crosslinking are responsible for the precipitation of spectrin in acidic buffer. Since hemolysis in hypotonic buffer at pH 6.0 yields ghosts with spicules and microvesicles, the structure of spectrin in intact cells might also be changed and lead to the clustering of transmembrane proteins and the aggregation of components of the cytoplasmic network.
Baumann
E
E
Institute of Anatomy, Friedrich Schiller University Jena, Germany.
Linss
W
W
Fröhner
M
M
Stoya
G
G
Richter
W
W
D002731:4-Chloromercuribenzenesulfonate; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure*; D005614:Freeze Fracturing; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007038:Hypotonic Solutions; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000097:blood* / Q000648:ultrastructure*; D008854:Microscopy, Electron; D011489:Protein Denaturation; D012995:Solubility; D013049:Spectrin / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature
D007038:Hypotonic Solutions; D046911:Macromolecular Substances; D008565:Membrane Proteins; D013049:Spectrin; D002731:4-Chloromercuribenzenesulfonate