Purification and molecular cloning of a novel calcium-binding protein, p26olf, in the frog olfactory epithelium

Olfactory adaptation requires the change of intracellular calcium concentration during stimuli. To contribute in the study of the molecular mechanism of calcium-dependent regulations in olfactory receptor cells, we isolated a novel 26-kDa Ca2+-binding protein named p26olf from the frog olfactory epithelium after four chromatographical steps. Based on the partial amino acid sequences of the proteolysed fragments of p26olf, we obtained a cDNA clone that encodes p26olf. The analysis of its amino acid sequence revealed that p26olf consists of two S-100-like regions aligned sequentially with a calculated molecular mass of 24,493. Northern blot analysis showed that p26olf is expressed in the frog olfactory epithelium and also in other tissues. Immunoreactivity against p26olf was detected in the cilia layer of the olfactory epithelium. These results suggest that p26olf is a dimeric form of S-100 proteins and is involved in the olfactory transduction or adaptation.