Actin in erythrocyte ghosts and its association with spectrin. Evidence for a nonfilamentous form of these two molecules in situ

@article{Tilney1975ActinIE,
  title={Actin in erythrocyte ghosts and its association with spectrin. Evidence for a nonfilamentous form of these two molecules in situ},
  author={Lewis G. Tilney and Patricia A. Detmers},
  journal={The Journal of Cell Biology},
  year={1975},
  volume={66},
  pages={508 - 520}
}
Actin was isolated from erythrocyte ghosts. It is identical to muscle actin in its molecular weight, net charge, ability to polymerize into filaments with the double helical morphology, and its decoration with heavy meromyosin (HMM). when erythrocyte ghosts are incubated in 0.1 mM EDTA, actin and spectrin are solubilized. Spectrin has a larger molecular weight than muscle myosin. When salt is added to the EDTA extract, a branching filamentous polymer is formed. However, when muscle actin and… CONTINUE READING

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Since filaments are not present in untreated erythrocyte ghosts , we conclude that erythrocyte actin and spectrin associate to form an anastomosing network beneath the erythrocyte membrane .
Since filaments are not present in untreated erythrocyte ghosts , we conclude that erythrocyte actin and spectrin associate to form an anastomosing network beneath the erythrocyte membrane .
Since filaments are not present in untreated erythrocyte ghosts , we conclude that erythrocyte actin and spectrin associate to form an anastomosing network beneath the erythrocyte membrane .
Since filaments are not present in untreated erythrocyte ghosts , we conclude that erythrocyte actin and spectrin associate to form an anastomosing network beneath the erythrocyte membrane .
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