Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin.
K Kato, S Goto, Y Inaguma, K Hasegawa… - Journal of Biological …, 1994 - ASBMB
A 20-kDa protein (p20) that had internal amino acid sequences highly similar to those of
alpha B crystallin was purified from rat and human skeletal muscle. p20 co-eluted with alpha
B crystallin and HSP27/28 during column chromatography on DEAE-Sepharose and on Bio-
Gel A-5m. p20 was separated from alpha B crystallin and HSP27/28 and was resolved into
two fractions, a minor first peak and a major second peak, by column chromatography on S-
Sepharose in the presence of 7 M urea. During chromatography on a column of Superdex …
alpha B crystallin was purified from rat and human skeletal muscle. p20 co-eluted with alpha
B crystallin and HSP27/28 during column chromatography on DEAE-Sepharose and on Bio-
Gel A-5m. p20 was separated from alpha B crystallin and HSP27/28 and was resolved into
two fractions, a minor first peak and a major second peak, by column chromatography on S-
Sepharose in the presence of 7 M urea. During chromatography on a column of Superdex …