Work

Visualization of the protein associations in the erythrocyte membrane skeleton.

Year: 1985

Type: article

Abstract: 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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.82.18.6153

Authors: T J Byers, D Branton

Institution: Harvard University

Language: English

Topic: Erythrocyte Function and Pathophysiology

Subfield: Physiology (medical)

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Heart, Lung, and Blood Institute, National Institute of General Medical Sciences

Awards: MOLECULAR STUDIES OF RED BLOOD CELL SPECTRIN, Joint Program in Molecules,Cells and Organisms