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.
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© 1992 Springer-Verlag Berlin Heidelberg
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Molday, R.S., Reid, D.M., Connell, G., Molday, L.L. (1992). Molecular Properties of the cGMP-gated Cation Channel of Rod Photoreceptor Cells as Probed with Monoclonal Antibodies. In: Hargrave, P.A., Hofmann, K.P., Kaupp, U.B. (eds) Signal Transduction in Photoreceptor Cells. Research Reports in Physics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76482-0_14
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DOI: https://doi.org/10.1007/978-3-642-76482-0_14
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