Rhein L D, Cagan R H
J Neurochem. 1983 Aug;41(2):569-77. doi: 10.1111/j.1471-4159.1983.tb04777.x.
Cilia isolated from the olfactory epithelium (olfactory rosettes) of rainbow trout (Salmo gairdneri) bind amino acids, which are odor stimuli to this species. We demonstrate that L-threonine, L-serine, and L-alanine bind to a common site, TSA, in the cilia preparation. All possible mixtures of two of the amino acids as competitors, with the third as the 3H-labeled ligand, were studied. The effect of two combined (unlabeled) competitors was always substantially less than additive compared with their actions singly. Along with additional inhibition studies using mixtures of inhibitors, the data show that the three odorants must interact with at least one common binding site, TSA. Binding of L-[3H]lysine to site L was unaffected by addition of L-threonine, L-serine, or L-alanine, establishing its independence from site TSA. L-Arginine inhibited binding of L-[3H]lysine, showing that both of these basic amino acids interact with site L. The data establish the presence, in trout olfactory cilia, of at least two separate and noninteracting populations of odorant binding sites, TSA and L.
从虹鳟鱼(Salmo gairdneri)的嗅觉上皮组织(嗅叶)分离出的纤毛能够结合氨基酸,而氨基酸是该物种的气味刺激物。我们证明,L-苏氨酸、L-丝氨酸和L-丙氨酸在纤毛制剂中结合到一个共同的位点TSA上。研究了以两种氨基酸作为竞争者、第三种氨基酸作为3H标记配体的所有可能混合物。与单独作用相比,两种联合(未标记)竞争者的作用总是明显小于相加作用。连同使用抑制剂混合物的其他抑制研究一起,数据表明这三种气味剂必须与至少一个共同的结合位点TSA相互作用。L-[3H]赖氨酸与位点L的结合不受L-苏氨酸、L-丝氨酸或L-丙氨酸添加的影响,表明其与位点TSA无关。L-精氨酸抑制L-[3H]赖氨酸的结合,表明这两种碱性氨基酸都与位点L相互作用。数据证实,在虹鳟鱼嗅觉纤毛中存在至少两个独立且不相互作用的气味剂结合位点群体,即TSA和L。