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[3H]催产素在雌性大鼠脑中的特异性结合。

Specific binding of [3H]oxytocin in the female rat brain.

作者信息

Ferrier B M, McClorry S A, Cochrane A W

出版信息

Can J Physiol Pharmacol. 1983 Sep;61(9):989-95. doi: 10.1139/y83-148.

DOI:10.1139/y83-148
PMID:6640435
Abstract

Because of demonstrated effects of oxytocin on some limbic system mediated behaviours, the specific binding of [3H]oxytocin to a plasma membrane containing fraction of rat limbic tissue has been studied. The binding of the microsomal fraction of estrogenized, female rat tissue was time dependent and saturable, with a Bmax of 2.5 X 10(-13) moles per milligram of protein and an apparent KD of 3.53 X 10(-8)M, and appeared to show positive cooperativity. The pH optimum of the binding was 6.0, close to the pH optimum for oxytocin-neurophysin binding; however, other results show the two types of binding to be different. The microsomal fraction did not appreciably degrade oxytocin under the conditions used for [3H]oxytocin binding. The distribution in limbic tissue of oxytocin-degrading activity and of individual enzymes capable of degrading oxytocin has been examined and an interplay of enzymes concentrated in different cell types is proposed.

摘要

由于已证实催产素对某些边缘系统介导的行为有影响,因此对[3H]催产素与大鼠边缘组织含质膜部分的特异性结合进行了研究。雌激素化的雌性大鼠组织微粒体部分的结合具有时间依赖性和饱和性,每毫克蛋白质的Bmax为2.5×10^(-13)摩尔,表观解离常数(KD)为3.53×10^(-8)M,并且似乎显示出正协同性。结合的最适pH为6.0,接近催产素-神经垂体素结合的最适pH;然而,其他结果表明这两种结合类型是不同的。在用于[3H]催产素结合的条件下,微粒体部分不会明显降解催产素。已研究了催产素降解活性以及能够降解催产素的各个酶在边缘组织中的分布,并提出了集中在不同细胞类型中的酶之间的相互作用。

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