Electrophoretic variation in low molecular weight lens crystallins from inbred strains of rats.

Analysis of rat lens soluble proteins by analytical isoelectric focusing detected two inherited electrophoretic differences in low molecular weight (LM) crystallins from inbred strains of rats(Rattus norvegicus). The polymorphic lens crystallins were shown to be similar to a genetically variant LM crystallin, LEN-1, previously described in mice(Mus musculus) and encoded on chromosome 1, at a locus linked toPep-3 (dipeptidase). Linkage analysis demonstrated that the rat crystallin locus was loosely linked toPep-3 at a recombination distance of 38±4.5 U. These data suggest the conservation of a large chromosomal region during the evolution of Rodentia and support the hypothesis that the γ-crystallins are evolving more rapidly than α- or β-crystallins.