Lens crystallins of invertebrates--diversity and recruitment from detoxification enzymes and novel proteins.

@article{Tomarev1996LensCO,
  title={Lens crystallins of invertebrates--diversity and recruitment from detoxification enzymes and novel proteins.},
  author={Stanislav I. Tomarev and Joram Piatigorsky},
  journal={European journal of biochemistry},
  year={1996},
  volume={235 3},
  pages={449-65}
}
The major proteins (crystallins) of the transparent, refractive eye lens of vertebrates are a surprisingly diverse group of multifunctional proteins. A number of lens crystallins display taxon-specificity. In general, vertebrate crystallins have been recruited from stress-protective proteins (i.e. the small heat-shock proteins) and a number of metabolic enzymes by a gene-sharing mechanism. Despite the existence of refractive lenses in the complex and compound eyes of many invertebrates… CONTINUE READING