THE ASSEMBLY STATE OF THE INTERMEDIATE FILAMENT PROTEINS DESMIN AND GLIAL FIBRILLARY ACIDIC PROTEIN AT LOW IONIC-STRENGTH

Authors
KOOIJMAN M VANAMERONGEN H TRAUB P VANGRONDELLE R BLOEMENDAL M
Citation
M. Kooijman et al., THE ASSEMBLY STATE OF THE INTERMEDIATE FILAMENT PROTEINS DESMIN AND GLIAL FIBRILLARY ACIDIC PROTEIN AT LOW IONIC-STRENGTH, FEBS letters, 358(2), 1995, pp. 185-188
Citations number
25
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
358
Issue
2
Year of publication
1995
Pages
185 - 188
Database
ISI
SICI code
0014-5793(1995)358:2<185:TASOTI>2.0.ZU;2-5
Abstract
The low ionic strength structures of the type III intermediate filamen t (IF) proteins desmin and glial fibrillary acidic protein (GFAP) have been studied by transient electric birefringence measurements. Flexib le 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 chan ge in the pH range studied. The results are compared,vith previous res ults on vimentin.