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.
