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S-100蛋白与突触体颗粒组分的特异性相互作用。S-100与其结合位点之间形成紧密复合物的证据。

The specific interaction of S-100 protein with synaptosomal particulate fractions. Evidence for the formation of a tight complex between S-100 and its binding sites.

作者信息

Donato R

出版信息

J Neurochem. 1981 Feb;36(2):532-7. doi: 10.1111/j.1471-4159.1981.tb01624.x.

Abstract

The dissociation of the 125I-labelled S-100 specifically bound to synaptosomal particulate fractions (SYN) has been studied under a variety of conditions after different association times. The results indicate that after a critical association time of about 20 min at 37 degrees C, the bound protein becomes progressively less accessible to the dissociating agents of conditions employed. These findings support the view that the partial irreversibility of the 125I-labelled S-100 binding to SYN could be due to the formation of a tight complex between the protein and its synaptosomal sites. These data are discussed mainly in relation to the particulate-bound fraction of native S-100.

摘要

在不同的结合时间后,在多种条件下研究了与突触体颗粒部分(SYN)特异性结合的125I标记的S-100的解离情况。结果表明,在37℃下约20分钟的关键结合时间后,结合的蛋白质对于所采用条件下的解离剂变得越来越难以接近。这些发现支持这样一种观点,即125I标记的S-100与SYN结合的部分不可逆性可能是由于该蛋白质与其突触体位点之间形成了紧密复合物。主要结合天然S-100的颗粒结合部分对这些数据进行了讨论。

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