O-Crystallin, arginine kinase and ferritin from the octopus lens.
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.
Zinovieva
R D
RD
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.
Piatigorsky
J
J
Tomarev
S I
SI
D000595:Amino Acid Sequence; D000818:Animals; D001122:Arginine Kinase / Q000302:isolation & purification*; D003459:Crystallins / Q000235:genetics / Q000302:isolation & purification*; D005293:Ferritins / Q000302:isolation & purification*; D007908:Lens, Crystalline / Q000378:metabolism*; D008969:Molecular Sequence Data; D049831:Octopodiformes / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000032:analysis
D003459:Crystallins; D012333:RNA, Messenger; D005293:Ferritins; D001122:Arginine Kinase