Visualization of the protein associations in the erythrocyte membrane skeleton.

AUTOR(ES)

Byers, T J

RESUMO

We have obtained clear images of the erythrocyte membrane skeleton from negatively stained preparations that originate directly from the intact cell but in which the spectrin meshwork is artificially spread to allow close inspection. Our procedure requires less than 2 min at 5 degrees C in phosphate buffers. We find 200-nm-long spectrin tetramers crosslinked by junctional complexes. Each junction contains a regular 37-nm rod, probably an actin oligomer of approximately 13 monomers. Densities appear at variable places in the meshwork but distinct globules occur with great frequency 78 nm from the spectrin tetramer's junctional insertion end, very close to the known binding site for ankyrin. Most frequently, five or six spectrin tetramers insert into each junction, producing a meshwork that displays remarkably regular long range order.

Documentos Relacionados

• Associations in the hominoid facial skeleton.
• Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton.
• Molecular defect in the sickle erythrocyte skeleton. Abnormal spectrin binding to sickle inside-our vesicles.
• Evidence that the middle T antigen of polyomavirus interacts with the membrane skeleton.
• Influence of network topology on the elasticity of the red blood cell membrane skeleton.