A structural comparison of tryptic fragments of three types of intermediate filaments.
We have compared tryptic fragments of three types of intermediate filaments, emphasizing structural characteristics as seen in the electron microscope. Variable, long alpha-helical rod fragments were found to be similar for keratin, neurofilaments and desmin filaments. Short rod fragments from keratin and neurofilaments appeared similar when observed by electron microscopy. Short rod fragments were not seen in desmin filament digests. In addition to these elongated particles, globular fragments, which have not been described previously, were obtained from all three types of intermediate filaments. These globular fragments were characterized by gel filtration and electron microscopy, and compared to globular proteins of known size using both methods. The diameter was about 6 nm and the molecular weight was estimated to be 50 000-60 000. These globular particles may comprise the short, nonhelical regions from several IF protein subunits, which are clustered into an interface in the intact filament or protofilaments.
Milam
L M
LM
Erickson
H P
HP
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003599:Cytoskeleton / Q000648:ultrastructure*; D003893:Desmin / Q000032:analysis; D006868:Hydrolysis; D007381:Intermediate Filament Proteins / Q000032:analysis*; D007382:Intermediate Filaments / Q000032:analysis / Q000648:ultrastructure*; D007633:Keratins / Q000032:analysis; D008854:Microscopy, Electron; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D013116:Spinal Cord / Q000032:analysis / Q000648:ultrastructure; D014357:Trypsin
D003893:Desmin; D007381:Intermediate Filament Proteins; D010446:Peptide Fragments; D007633:Keratins; D014357:Trypsin