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.
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