A high performance liquid chromatography method to obtain rat epidermal filaggrin

Sodium pyrophosphate-glycerol buffer, a non-denaturing buffer has been used to solubilize epidermal proteins. The extracted proteins are different in their electrophoretic profile in various mammalian species, 47 K in rat and guinea pig, 31 K and 60 K in mouse and 43 K and 60 K proteins in human epi...

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Veröffentlicht in:	Biochemical and biophysical research communications 1985-11, Vol.132 (3), p.1196-1203
Hauptverfasser:	Bhatnagar, Gopal M., Supakar, Prakash C., Bhatnagar, Yogendra M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Animals Chromatography, High Pressure Liquid epidermis Epidermis - analysis filaggrin Guinea Pigs high-performance liquid chromatography Humans Intermediate Filament Proteins - analysis Intermediate Filament Proteins - isolation & purification Mice Mice, Inbred BALB C Molecular Weight Proteins - isolation & purification Rats Rats, Inbred Strains
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Beschreibung
Zusammenfassung:	Sodium pyrophosphate-glycerol buffer, a non-denaturing buffer has been used to solubilize epidermal proteins. The extracted proteins are different in their electrophoretic profile in various mammalian species, 47 K in rat and guinea pig, 31 K and 60 K in mouse and 43 K and 60 K proteins in human epidermis were most predominant. Electrophoretic analyses show synthesis of new proteins as a function of age in rat tissue. Purification of the major rat protein fraction was achieved using a reverse phase high-performance liquid chromatography using a gradient of 5–50% acetonitrile. Based upon the molecular size, amino acid data and immunodiffusion analyses, we conclude the purified rat protein to be filaggrin.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(85)91933-3