嗅觉接收的分子机制。IV. 大鼠嗅觉上皮中樟脑受体的一些生化特性。

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

作者信息

Fesenko E E, Novoselov V I, Krapivinskaya L D

出版信息

Biochim Biophys Acta. 1979 Oct 18;587(3):424-32. doi: 10.1016/0304-4165(79)90446-x.

Abstract

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.

摘要

对来自大鼠嗅上皮的受体元件的一些参数进行了评估；其特点是对樟脑具有高亲和力（KD = 1.5×10⁻⁹ M）。Triton X - 100对[³H]樟脑的结合没有显著影响。核糖核酸酶和磷脂酶C均不影响[³H]樟脑结合活性。链霉蛋白酶和胰蛋白酶分别使[³H]樟脑结合活性丧失65%和40%。巯基试剂使[³H]樟脑的结合降低5 - 8倍。通过等电聚焦测定，用Triton X - 100溶解的受体的等电点为4.8。通过凝胶电泳测定的受体分子量约为120000。有人提出，樟脑受体是一种含有巯基且在嗅觉接收中起关键作用的膜蛋白。