Subunit structure of the mouse epidermal keratin filament.
The two proteins which are the subunits of mouse epidermal keratin filaments have been isolated from fully differentiated epidermis (stratum corneum), viable differentiating cells and cells grown in culture. The proteins have molecular weights of 68 000 and 60 000, consist of families of very similar species, have common N-terminal (N-acetylserine) and C-terminal (glycine) residues, contain 35--40% alpha-helix and are immunologically cross-reacting. In mixtures, the two proteins polymerize in vitro into native-type keratin filaments that are 70--80 angstrom in diameter, up to 30 micrograms long, possess a characteristic alpha-type X-ray diffraction pattern and contain the subunits in the precise molar ratio of 1 : 2 or 2 : 1.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000831:Animals, Newborn; D005779:Immunodiffusion; D007124:Immunoenzyme Techniques; D007633:Keratins / Q000302:isolation & purification; D046911:Macromolecular Substances; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D011487:Protein Conformation; D012867:Skin / Q000032:analysis*
D000596:Amino Acids; D046911:Macromolecular Substances; D007633:Keratins