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 high affinity for camphor (KD = 1.5. x 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.
D000818:Animals; D002164:Camphor; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004848:Epithelium / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D009831:Olfactory Mucosa / Q000032:analysis*; D011092:Polyethylene Glycols; D011485:Protein Binding; D051381:Rats; D011984:Sensory Receptor Cells / Q000032:analysis*; D013439:Sulfhydryl Reagents
D013439:Sulfhydryl Reagents; D011092:Polyethylene Glycols; D002164:Camphor