Improved resolution of calf lens β-crystallins

Abstract

Native crystallins isolated from the calf lens cortex were separated by a modified gel filtration procedure. The constituent polypeptides were then separated by gel electrophoresis. It was found, that, when gel filtration was performed in the presence of 1 m-NaCl or alternatively at room temperature, a 60 000 dalton constituent, consisting mainly of βB p, was released from β H leaving a “core β H” of about 180 000 daltons. The β L fraction was partially resolved into several sizes of protein aggregates.