Enzymology and Molecular Biology of Carbonyl Metabolism 4

@inproceedings{Lipsky1993EnzymologyAM,
  title={Enzymology and Molecular Biology of Carbonyl Metabolism 4},
  author={James J. Lipsky and Norman E. Sl{\'a}dek and B. Fritzsch and Ronald G. Lindah and Giuliana Muzi and Dennis R. Petersen},
  booktitle={Advances in Experimental Medicine and Biology},
  year={1993}
}
The refractive properties of the eye lens are determined by abundant soluble structural proteins known as crystallins. While some crystallins are common to most vertebrates, others are abundant only in groups of related species. These taxon-specific crystallins all tum out to be enzymes, apparently recruited by modification of gene expression without prior gene duplication. They include f)-crystallin, accounting for up to 25% of protein in elephant shrew lenses and apparently identical to… CONTINUE READING