We have isolated a novel secretory 28-kDa protein which is an abundant component of the rat olfactory mucosa. The partial sequence of the 28-kDa protein has been determined. The amino acid sequence of the 28-kDa protein is similar to that of non-selenium glutathione peroxidase from bovine ciliary body. The 28-kDa protein catalyzed decomposition of the hydrogen peroxide as well as organic hydroperoxides by reduced glutathion and seems to be a member of the glutathion peroxidases family.
The rat olfactory epithelium contains a specific water-soluble 45-kDa protein. This protein is recognized by anti-peptide antibodies which react with alpha-subunits of the known G-proteins. The 45-kDa protein has been isolated using DEAE-chromatography and gel-exclusion chromatography. The content of 45-kDa protein is about 2% of the total soluble proteins of the olfactory mucosa and it is located at the mucociliary surface. According to photo-affinity labeling, the 45-kDa protein possesses a high affinity to GTP and exhibits low GTP hydrolytic activity. The functions of the 45-kDa protein are discussed.
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