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Journal of Neuroscience, Vol 6, 1962-1969, Copyright © 1986 by Society for Neuroscience
A partially purified preparation of isolated chemosensory cilia from the olfactory epithelium of the bullfrog, Rana catesbeiana
RR Anholt, U Aebi and SH Snyder
Cilia at the tips of dendritic processes of olfactory receptor cells are
the sites of initial recognition and transduction events in olfactory
reception. We have detached cilia from the olfactory epithelium of the
bullfrog, Rana catesbeiana, via a calcium shock and partially purified them
in high yield (226 +/- 19 micrograms protein/frog, n = 14) by sucrose
gradient centrifugation. The cilia appear to undergo osmotic lysis during
the isolation procedure, forming isolated axonemal structures and ciliary
plasma membrane vesicles with diameters of 100-500 nm and an internal
volume of 2.3 +/- 0.5 microliter/mg protein. PAGE in SDS reveals
approximately 30 protein bands, among which cytoskeletal components, such
as tubulin and actin, are readily identifiable by immunoblotting.
Approximately 15 glycoprotein bands reactive with concanavalin A are
discernible with major glycopeptides at apparent molecular weights of
56-65, 95, and 116 kDa. In contrast to olfactory cilia, respiratory cilia,
isolated from the palate of the frog, do not contain the prominent
glycopeptides observed for olfactory cilia. The 56-65 kDa glycopeptide
region reacts with antiserum against chick kidney, Na+/K+-ATPase, and
contains the beta subunit of this enzyme. In addition, we have identified
the alpha and beta subunits of a guanine nucleotide-binding protein
(G-protein) in the olfactory cilia preparation. This preparation of
isolated olfactory cilia from Rana catesbeiana represents a readily
accessible model system for studies of initial events in chemosensory
recognition and signal transduction in the olfactory system.
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