O-Crystallin, arginine kinase and ferritin from the octopus lens. |
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Authors: | R D Zinovieva J Piatigorsky S I Tomarev |
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Institution: | Laboratory of Molecular and Developmental Biology, National Eye Institute, National Institutes of Health, NIH, Bldg. 6, Room 2A04, 6 Center Dr. MSC 2730, Bethesda, MD 20892-2730, USA. |
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Abstract: | Three proteins have been identified in the eye lens of the octopus, Octopus dofleini. A 22 kDa protein comprising 3-5% of the soluble protein of the lens is 35-43% identical to a family of phosphatidylethanolamine-binding proteins of vertebrates. Other members of this family include the immunodominant antigen of the filarial parasite, Onchocerca volvulus, putative odorant-binding proteins of Drosophila and a protein with unknown function of Caenorhabditis elegans. We have called this protein O-crystallin on the basis of its abundance in the transparent lens. O-Crystallin mRNA was detected only in the lens. Two tryptic peptides of another octopus lens protein, less abundant than O-crystallin, showed 80% identity to arginine kinase of invertebrates, a relative of creatine kinase of vertebrates. Finally, ferritin cDNA was isolated as an abundant cDNA from the octopus lens library. Northern blots showed that ferritin mRNA is not lens-specific. |
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