O-Crystallin, arginine kinase and ferritin from the octopus lens.
Biochim Biophys Acta
; 1431(2): 512-7, 1999 May 18.
Article
en En
| MEDLINE
| ID: mdl-10350626
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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Banco de datos:
MEDLINE
Asunto principal:
Arginina Quinasa
/
Cristalinas
/
Ferritinas
/
Cristalino
/
Octopodiformes
Límite:
Animals
Idioma:
En
Año:
1999
Tipo del documento:
Article