Novel 28‐kDa secretory protein from rat olfactory epithelium
- 26 February 1996
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 381 (1-2), 12-14
- https://doi.org/10.1016/0014-5793(96)00071-3
Abstract
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 glutathione and seems to be a member of the glutathion peroxidase family.Keywords
This publication has 11 references indexed in Scilit:
- Water‐soluble GTP‐binding protein from rat olfactory epitheliumFEBS Letters, 1994
- Olfactory neurones expressing distinct odorant receptor subtypes are spatially segregated in the nasal neuroepitheliumCell and tissue research, 1994
- A novel multigene family may encode odorant receptors: A molecular basis for odor recognitionCell, 1991
- Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary bodyExperimental Eye Research, 1990
- Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzymeArchives of Biochemistry and Biophysics, 1987
- Perireceptor and receptor events in vertebrate olfactionProgress in Neurobiology, 1984
- [53] Glutathione peroxidase and hydroperoxidesMethods in Enzymology, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970