Identification of proteolytic activities in ROS 17/2.8 cell lysates which cleave peptide substrates for protein kinase C-mediated phosphorylation.
Identification of proteolytic activities in ROS 17/2.8 cell lysates which cleave peptide substrates for protein kinase C-mediated phosphorylation.
复制标题
鉴定 ROS 17/2.8 细胞裂解物中的蛋白水解活性，该裂解物可裂解蛋白激酶 C 介导的磷酸化的肽底物。
DOI：
10.1016/s0945-053x(96)90128-6
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Harrison,P
中科院分区：
文献类型：
--
作者：
GuidonJr,PT;Harrison,P
我们在大鼠成骨性骨肉瘤细胞系ROS17/2.8的细胞裂解物中观察到两种蛋白分解活性，它们能够切割多肽底物以实现蛋白激酶C介导的磷酸化，以及其他含有类似序列的多肽。这两种活性都被一种系列蛋白酶抑制剂Pefabloc抑制，而其中一种活性被EDTA或抑肽酶抑制。蛋白水解酶抑制剂胃抑素、贝斯汀、E-、亮肽素和磷酰胺都不能阻断这两种蛋白分解活性。
We have observed two proteolytic activities in cell lysates from the rat osteoblastic osteosarcoma cell line ROS 17/2.8 which are capable of cleaving a peptide substrate for protein kinase C-mediated phosphorylation, and other peptides containing similar sequences. Both activities are inhibited by Pefabloc, a serie protease inhibitor, while one of the activities is inhibited by either EDTA or aprotinin. The protease inhibitors pepstatin, bestatin, E-64, leupeptin and phosphoramidon do not block either of these proteolytic activities.