Towards a human crystallin map. Two-dimensional gel electrophoresis and computer analysis of water-soluble crystallins from normal and cataractous human lenses.
This paper describes a first approach to establish a master data base of human lens crystallins obtained by computer analysis of standardized two-dimensional lenticular protein patterns. To facilitate the eventual identification of the spots, the major crystallins have been separated into alpha-, beta H-, beta L- and gamma-crystallin fractions by gel filtration. The authors encourage colleague investigators to collaborate in a common effort in order to arrive eventually at a two-dimensional gel data base of all lenticular proteins.
Bloemendal
H
H
Department of Biochemistry, University of Nijmegen, The Netherlands.
Van de gaer
K
K
Benedetti
E L
EL
Dunia
I
I
Steely
H T
HT
D000375:Aging / Q000378:metabolism; D002386:Cataract / Q000378:metabolism*; D002648:Child; D003459:Crystallins / Q000032:analysis*; D001330:Electronic Data Processing / Q000379:methods*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D006801:Humans; D015151:Immunoblotting; D007223:Infant; D007908:Lens, Crystalline / Q000737:chemistry*; D008875:Middle Aged; D012995:Solubility
D003459:Crystallins