This thesis is an investigation into the potential mechanisms that could explain the olfactory sensitivity to thiol compounds ~ought to be conserved across mammalian species. Proteomics techniques were employed as unbiased tools to search for highly conserved proteins in olfactory cilia theoretically capable of strong interactions with thiol odorants. Comparisons of the protein profiles and directed protein labelling studies of olfactory cilia from three mammalian species - the house mouse (Mus musculus), the rat (Rattus norvegicus) and the sheep (Ovis aries) - and respiratory cilia preparations from the rat enabled the identification of cytoskeletal proteins and olfactory receptors as potential targets for sulphydryl-mediated thiol odorant interactions. It is therefore predicted that olfactory detection of thiol odorants utilises a traditional olfactory receptor conserved across mammalian. species, the observed thiol sensitivity potentially a byproduct of a strong interaction between odorant and receptor. This study also represents the first broad ranging study of the protein complement of mammalian olfactory cilia derived from the three model species. The characterisation of olfactory and respiratory cilia proteomes from multiple mammalian species has highlighted a novel family of putative pheromone binding proteins uniquely associated with mouse olfactory cilia preparations. It has also provided further evidence for the ongoing investigations of the functions of odorant-binding proteins and annexins.