Purification and characterization of a gamma crystallin from mouse lenses

Abstract

A γ-crystallin has been purified by a two-step column chromatography from an extract of water soluble lens proteins from (101/E1XC3H/E1)F₁ mice. About 17% of the water soluble lens protein in normal mice is represented by this γ-crystallin. The protein has been shown to be absent in cataractous lenses of Nop/+ mice after isoelectric focusing of water soluble lens proteins. It has a MW of 20,000. Amino acid analysis reveals the occurence of eight cystein residues, which is considered to be high compared to other crystallins. The protein might play an important role in cataractogenesis.