Molecular mechanisms of olfactory reception IV. Some biochemical characteristics of the camphor receptor from rat olfactory epithelium

Some parameters of the receptor element from the rat olfactory epithelium are evaluated; it is characterized by a high affinity for camphor (K_D = 1.5 · 10^?9 M). Triton X-100 has no marked effect on the binding of ³H]camphor. Neither RNAase nor phospholipase C affected ³H]camphor-binding activity. Pronase and trypsin abolished ³H]camphor binding activity by 65 and 40%, respectively. Sulfhydryl reagents decrease the binding of ³H]camphor by a factor of 5–8. The isoelectric point of the receptor solubilized with Triton X-100 is 4.8, as determined by isoelectric focusing. The molecular weight of the receptor as determined by gel electrophoresis is about 120 000. It is proposed that the camphor receptor is a membrane protein containing sulfhydryl groups and playing a key role in olfactory reception.