Abstract
Soluble proteins from the whole lens of Rana catesbeiana at tadpole and adult stages were examined by cellulose acetate electrophoresis. The soluble proteins isolated from the periphery (cortex) and the core (nucleus) of the adult lens were also examined. Electrophoresis for 2 hours showed distinct quantitative differences between the profiles of tadpole and adult frog stages, while a similarity was noted between the whole tadpole lens and the nucleus of the adult lens. Electrophoresis for 50 minutes revealed distinct alpha crystallin fractions, differing in electrophoretic mobility and relative protein content, in adult nucleus, in adult cortex, and in tadpole lens preparations.
Published Version
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