Fesenko E E, Novoselov V I, Bystrova M F
Institute of Biological Physics, Academy of Sciences, Pushchino, Moscow Region, U.S.S.R.
Biochim Biophys Acta. 1988 Jan 22;937(2):369-78. doi: 10.1016/0005-2736(88)90259-3.
The specific membrane glycoproteins with high affinity for camphor and decanal were isolated from rat olfactory epithelium. Antibodies to these glycoproteins inhibited both the electroolfactogram and the binding of odorants. The enzyme immunoassay has shown these glycoproteins to be present in the olfactory epithelium of rat, mouse, guinea-pig and hamster but not in that of frog and carp. The molecular mass of the odour-binding glycoproteins from rat olfactory epithelium solubilized by Triton X-100 was approx. 140 kDa. They consisted of two subunits (88 and 55 kDa). The 88 kDa subunit was capable of binding odorants. The data obtained suggest that the glycoproteins isolated have some properties that make them plausible candidates for olfactory receptor molecules.