title: Soluble proteins from fowl feather keratin. III. Isolation and characteristics of some calamus proteins.
abstract: The main fraction, GF-3, separated from SCM-proteins of fowl feather calamus by gel filtration, was separated into seven peaks, C-1 to C-7, by ion exchange chromatography on a DEAE-cellulose column. Each fraction was found to contain two components by polyacrylamide gel electrophoresis. In order to separate these two components, recycling gel filtration on a Sephadex G-75 column was carried out. Two peaks separated from each of four fractions, C-3 to C-6, were termed C-3a and -3b, C-4a and -4b, and so on. Electrophoretic results showed that all the fractions were single protein components. Components a and b of a particular fraction had almost identical electric charge and slightly different molecular size. All components in Group a (C-3a to C-6a) had similar amino acid compositions except for SCM-cysteine content, and similar results were obtained for Group b (C-3b to C-7b). Groups a and b had significantly different amino acid compositions.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001717:Birds; D002645:Chickens; D002850:Chromatography, Gel; D005241:Feathers; D007633:Keratins; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D011506:Proteins; D007633:Keratins