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Abstract

A gamma-crystallin has been purified by a two-step column chromatography from an extract of water soluble lens proteins from (101/ElxC3H/El)F-l 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.

Additional information

Authors: DORIA R, INSTITUT FUER GENETIK AND INSTITUT FUER TOXIKOLOGIE UND BIOCHEMIE, GESELLSCHAFT FUER STRAHLEN- UND UMWELTFORSCHUNG MBH, MUENCHEN, NEUHERBERG (GERMANY);GRAW J, INSTITUT FUER GENETIK AND INSTITUT FUER TOXIKOLOGIE UND BIOCHEMIE, GESELLSCHAFT FUER STRAHLEN- UND UMWELTFORSCHUNG MBH, MUENCHEN, NEUHERBERG (GERMANY);MAIER K INSTITUT FUER GENETIK AND INSTITUT FUER TOXIKOLOGIE UND BIOCHEMIE, GESELLSCHAFT FUER STRAHLEN- UND UMWELTFORSCHUNG MBH, MUENCHEN, NEUHERBERG (GERMANY), INSTITUT FUER GENETIK AND INSTITUT FUER TOXIKOLOGIE UND BIOCHEMIE, GESELLSCHAFT FUER STRAHLEN- UND UMWELTFORSCHUNG MBH, MUENCHEN, NEUHERBERG (GERMANY)
Bibliographic Reference: CURRENT EYE RESEARCH, VOL. 3 (1984), NO. 5, PP. 723-728
Record Number: 1989123026800 / Last updated on: 1987-01-01
Category: PUBLICATION
Available languages: en