| First Author | Maeda T | Year | 2000 |
| Journal | FEBS Lett | Volume | 470 |
| Issue | 3 | Pages | 336-40 |
| PubMed ID | 10745092 | Mgi Jnum | J:61477 |
| Mgi Id | MGI:1355031 | Doi | 10.1016/s0014-5793(00)01334-x |
| Citation | Maeda T, et al. (2000) Purification and characterization of bovine cone arrestin (cArr). FEBS Lett 470(3):336-40 |
| abstractText | To elucidate the quenching mechanism of phototransduction in vertebrate cone photoreceptors, a cDNA clone encoding cone specific arrestin (cArr) was isolated from a bovine retinal cDNA library using a human cArr cDNA probe. Affinity-purified anti-peptide antibody specific to cArr was prepared. Immunohistochemical staining displayed specific labeling of cArr in cone photoreceptors and immunoblotting identified a 46 kDa protein band. We purified cArr from bovine retinas by sequential column chromatography using DEAE-cellulose, gel filtration and mono Q columns. Binding studies revealed no binding of cArr to rhodopsin regardless of whether it was bleached and/or phosphorylated. cArr also failed to bind to heparin-Sepharose under conditions which rod arrestin (rArr) bound to the column. The present data suggest that cArr may play a role in the quenching of phototransduction in cone photoreceptors and that its activity therein is different to that of rArr. |
