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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)

Abstract

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.

Keywords

Unbind Fraction Sepharose Column Disk Membrane Immobilon Membrane Channel Polypeptide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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