The assembly state of the intermediate filament proteins desmin and glial fibrillary acidic protein at low ionic strength

FEBS Letters

Kooijman, Martin³  Traub, Peter²  van Amerongen, Herbert³  van Grondelle, Rienk³  Bloemendal, Michael¹ 

[1]Department of Protein and Molecular Biology, Royal Free Hospital School of Medicine, Rowland Hill Street, London, NW3 2PF, UK

[2]Max Planck Institute for Cell Biology, D68526 Ladenburg/Heidelberg, Germany

[3]Department of Biophysics, Free University, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands

关键词: Intermediate filament protein;    Desmin;    Glial fibrillary acidic protein;    Protein aggregation;    Transient electric birefringence;   

DOI  :  10.1016/0014-5793(94)01419-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The low ionic strength structures of the type III intermediate filament (IF) proteins desmin and glial fibrillary acidic protein (GFAP) have been studied by transient electric birefringence measurements. Flexible dimers with a length of around 45 nm, particles with a length of 68 ± 6 nm (presumably tetramers and hexamers) and larger aggregates of 108 ± 19 nm are found. GFAP has an increased tendency to aggregate upon lowering of the pH. The aggregation state of desmin does not change in the pH range studied. The results are compared with previous results on vimentin.

【 授权许可】

Unknown