Purification and characterization of bovine cone arrestin (cArr)

FEBS Lett. 2000 Mar 31;470(3):336-40. doi: 10.1016/s0014-5793(00)01334-x.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arrestin / chemistry
  • Arrestin / genetics
  • Arrestin / isolation & purification*
  • Arrestin / metabolism*
  • Cattle
  • Chromatography, Affinity
  • Cloning, Molecular
  • Heparin / metabolism
  • Humans
  • Molecular Sequence Data
  • Molecular Weight
  • Phosphorylation
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Retinal Cone Photoreceptor Cells / chemistry*
  • Retinal Cone Photoreceptor Cells / cytology
  • Rhodopsin / metabolism
  • Sequence Alignment


  • Arrestin
  • Recombinant Proteins
  • Heparin
  • Rhodopsin