Subunit structure of the mouse epidermal keratin filament. Biochim Biophys Acta 1979 Mar 27;577(1):11-21
Date
03/27/1979Pubmed ID
106897DOI
10.1016/0005-2795(79)90003-5Scopus ID
2-s2.0-0018424723 (requires institutional sign-in at Scopus site) 52 CitationsAbstract
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.
Author List
Steinert PM, Idler WW, Poirier MC, Katoh Y, Stoner GD, Yuspa SHMESH terms used to index this publication - Major topics in bold
Amino AcidsAnimals
Animals, Newborn
Immunodiffusion
Immunoenzyme Techniques
Keratins
Macromolecular Substances
Mice
Mice, Inbred BALB C
Molecular Weight
Protein Conformation
Skin
