Purification and characterization of a gamma crystallin from mouse lenses.
A gamma-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 gamma-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 occurrence of eight cystein residues, which is considered to be high compared to other crystallins. The protein might play an important role in cataractogenesis.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002845:Chromatography; D003459:Crystallins / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D007908:Lens, Crystalline / Q000032:analysis*; D008297:Male; D051379:Mice
D000596:Amino Acids; D003459:Crystallins