Purification and characterization of an inhibitor protein with cytochalasin-like activity from bovine adrenal medulla.
Purification and characterization of an inhibitor protein with cytochalasin-like activity from bovine adrenal medulla.
复制标题
从牛肾上腺髓质中纯化和表征具有细胞松弛素样活性的抑制剂蛋白。
DOI：
10.1016/0304-4165(81)90118-5
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
Lin,S
中科院分区：
文献类型：
--
作者：
Grumet,M;Lin,S
从牛肾上腺髓质中获得了一种具有细胞松弛素样活性的蛋白制剂。sds -聚丙烯酰胺凝胶电泳和Sephacryl S-200色谱柱分析表明，抑制剂活性与90000道尔顿多肽一致。抑制剂降低了[3H]细胞松弛素B与肌动蛋白核的高亲和力结合，显然是与药物竞争同一结合位点。在亚化学计量水平上，抑制剂对肌动蛋白丝的伸长和体外细胞提取物的肌动蛋白依赖性凝胶化有强有力的影响。这些结果表明，抑制剂可能参与控制肌动蛋白丝组装和肾上腺髓质的相互作用。
A protein preparation with cytochalasin-like activity has been obtained from bovine adrenal medulla. Analysis by electrophoresis in SDS-polyacrylamide gels and chromatography in a Sephacryl S-200 column indicated that the inhibitor activity coincided with a 90 000 dalton polypeptide. The inhibitor decreased high-affinity binding of [3H]cytochalasin B to actin nuclei, apparently by competing with the drug for thesame binding site. At substoichometric levels, the inhibitor had a potent effect on actin filament elongation and on actin-dependent gelation of cell extracts in vitro. These results suggest that the inhibitor may be involved in the control of actin filament assembly and interaction in the adrenal medulla.