Molecular Properties of the cGMP-gated Cation Channel of Rod Photoreceptor Cells as Probed with Monoclonal Antibodies

  • R. S. Molday
  • D. M. Reid
  • G. Connell
  • L. L. Molday
Conference paper
Part of the Research Reports in Physics book series (RESREPORTS)


Monoclonal antibodies have been generated against different epitopes of the cGMP-gated channel of bovine rod outer segments for use as probes to study the molecular properties of this channel protein. These monoclonal antibodies selectively labeled a 63 kDa polypeptide in both bovine rod outer segment membranes and purified channel preparations and crossreact with a 63 kDa polypeptide in rod outer segment preparations from other mammalian retinas. Immunoprecipitation studies have confirmed the identity of the 63 kDa protein as the cGMP-gated channel of rod outer segment membranes and have shown that the channel is associated with a 240 kDa protein. Solid phase radioimmune competition studies on isolated rod outer segment disks and plasma membranes have indicated that the plasma membrane has a channel density which is over 200 times greater than that in disk membranes. A monoclonal antibody against a synthetic peptide also been developed and used to study the properties of the N-terminal segment of the channel.


Unbind Fraction Sepharose Column Disk Membrane Immobilon Membrane Channel Polypeptide 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • R. S. Molday
    • 1
  • D. M. Reid
    • 1
  • G. Connell
    • 1
  • L. L. Molday
    • 1
  1. 1.Department of BiochemistryUniversity of British ColumbiaVancouverCanada

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