Antisera to synthetic peptides of bovine rhodopsin: use as site-specific probes of disc membrane changes in retinal dystrophic dogs

Biochem Biophys Res Commun. 1985 Oct 15;132(1):438-44. doi: 10.1016/0006-291x(85)91041-1.


Based on the amino acid sequence of bovine rhodopsin, five peptides corresponding to the carboxyl terminus and one loop region have been synthesized. Rabbit antisera to these peptides recognize rhodopsin in whole bovine and dog retinas. Antisera were used to detect differences in specific regions of rhodopsin in dystrophic vs normal dog retinas. As detected on both "dot blots" and Western blots, rhodopsin from retinas of dystrophic dogs has a reduced reaction with antisera to peptides, Rhod-4 and Rhod-10 (# 341-348 and 232-239, respectively). Since these sites on rhodopsin are possible binding sites for transducin and rhodopsin kinase, an alteration in these regions would have profound effects in the dystrophic state.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle
  • Dog Diseases / metabolism
  • Dogs
  • Eye Proteins*
  • G-Protein-Coupled Receptor Kinase 1
  • Immune Sera*
  • Membrane Proteins / metabolism
  • Muscular Dystrophy, Animal / metabolism
  • Protein Kinases / metabolism
  • Radioimmunoassay
  • Retina / analysis
  • Retinal Pigments / chemical synthesis*
  • Rhodopsin / chemical synthesis*
  • Rhodopsin / immunology
  • Transducin


  • Eye Proteins
  • Immune Sera
  • Membrane Proteins
  • Retinal Pigments
  • Rhodopsin
  • Protein Kinases
  • G-Protein-Coupled Receptor Kinase 1
  • Transducin