High-Sulphur Proteins From a-Keratins I. Heterogeneity of the Proteins From Mouse Hair
- 1 January 1976
- journal article
- research article
- Published by CSIRO Publishing in Australian Journal of Biological Sciences
- Vol. 29 (2) , 1-10
- https://doi.org/10.1071/bi9760001
Abstract
The heterogeneity of the reduced and S-carboxymethylated high-sulphur protein fraction from mouse hair has been examined by chromatography and polyacrylamide gel electrophoresis at pH values above and below the isoelectric region. Considerable heterogeneity is observed both in size (molecular weight range 12000-45000) and in charge. Amino acid analysis of a number of column chromatographic fractions shows the high-sulphur proteins to be largely composed of proteins with a carboxymethy1cysteine content above 25 residues per 100 residues and a pronounced heterogeneity in arginine content. Their chromatographic behaviour is similar to that observed for the ultra-high-sulphur proteins from wool.Keywords
This publication has 4 references indexed in Scilit:
- The dietary-regulated biosynthesis of high-sulphur wool proteinsBiochemical Journal, 1966
- A comparative study of high-sulphur proteins from α-keratinsComparative Biochemistry and Physiology, 1965
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- The Isolation and Properties of Some Soluble Proteins From WoolAustralian Journal of Biological Sciences, 1964