title: Classification of rat lens crystallins and identification of proteins encoded by rat lens mRNA.
abstract: Endogenous rat lens crystallins have been separated by gel filtration into four fractions, alpha, beta H, beta L and gamma-crystallin. Elution patterns of soluble lens proteins from animals of different ages show a relative decrease of beta H and gamma-crystallin during aging. Conversely the relative amounts of alpha and beta L-crystallin are enhanced. The rat crystallin subunits from the four fractions were characterized by one-dimensional and two-dimensional gel electrophoretic techniques. From the results a classification could be derived and a nomenclature for the soluble rat lens proteins is proposed. The products synthesized by rat lens mRNAs in a heterologous cell-free system have also been characterized. Co-electrophoresis of the radioactive products synthesized de novo together with the isolated unlabeled protein fractions on two-dimensional gels shows the relation between primary gene products and their posttranslationally modified derivatives.
mesh_terms: D000375:Aging; D000818:Animals; D003459:Crystallins / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D007908:Lens, Crystalline / Q000254:growth & development / Q000378:metabolism*; D046911:Macromolecular Substances; D008970:Molecular Weight; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics*; D051381:Rats
chemical_list: D003459:Crystallins; D046911:Macromolecular Substances; D012333:RNA, Messenger