ZINC ION BINDING TO HUMAN-BRAIN CALCIUM-BINDING PROTEINS, CALMODULIN AND S100B PROTEIN
ZINC ION BINDING TO HUMAN-BRAIN CALCIUM-BINDING PROTEINS, CALMODULIN AND S100B PROTEIN
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DOI：
10.1016/0006-291x(83)90681-2
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发表时间：
1983-01-01
影响因子：
3.1
通讯作者：
GERARD, D
中科院分区：
文献类型：
--
作者：
BAUDIER, J;HAGLID, K;GERARD, D
比较研究了Zn~（2+）与人脑钙调素和S100b蛋白的结合特性。钙调蛋白的特征在于2组Zn结合位点，Kd范围为8. 10-5至3.10 - 4M。S100b蛋白还具有2组Zn~（2+）结合位点，且具有更高的亲和力。Kd = 10 - 7至10 - 6 M。S100b蛋白不应仅被认为是钙结合蛋白，还应被认为是锌结合蛋白。Zn~（2+）参与了S100蛋白的功能。
Comparative studies were performed on the binding properties of Zn2+ to human brain calmodulin and S100b protein. Calmodulin is characterized by 2 sets of Zn binding sites, with Kd ranging from 8 .cntdot. 10-5 to 3.10-4 M. The S100b protein also exhibited 2 sets of Zn2+ binding sites, with a much higher affinity. Kd = 10-7 to 10-6 M. S100b protein should no longer be considered only as a Ca2+ binding protein but also as a Zn binding protein. Zn2+ are apparently involved in the functions of the S100 proteins.