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首页> 外文期刊>Journal of Cellular Physiology >Peptide bond cleavage site determination of novel proteolytic enzymes found in ROS 17/2.8 cell lysates.
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Peptide bond cleavage site determination of novel proteolytic enzymes found in ROS 17/2.8 cell lysates.

机译：肽键裂解位点的小说蛋白水解酶在细胞ROS 17/2.8找到lysates。

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摘要

We have identified proteolytic activities in the rat osteoblastic osteosarcoma cell line ROS 17/2.8 which are capable of cleaving a peptide substrate for protein kinase C-mediated phosphorylation (PSPKC, Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys). Using polyacrylamide gel electrophoresis conditions similar to those used to resolve small molecular weight proteins, the peptide bonds of PSPKC which are cleaved by the proteolytic activities present in ROS 17/2.8 cell lysates have been determined. These activities cleave the Ser-Arg, Thr-Leu, and Ser-Val peptide bonds. To date, no proteolytic activities present in osteoblast cell lysates have been described with the aforementioned peptide bond specificities, suggesting that these activities are novel. The PSPKC-cleaved peptide fragment pattern generated was similar for several different osteoblast cell lysates. Lysates generated from different rat tissues were also able to cleave PSPKC, but the peptide fragment pattern generated by ROS 17/2.8 cell lysatesappeared to be unique amongst these tissues.
机译：我们已经确定了蛋白水解活动大鼠成骨细胞的骨肉瘤细胞系ROS17/2.8能够裂开一个肽蛋白激酶C-mediated生长的基质磷酸化(PSPKCPro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys)。用聚丙烯酰胺凝胶电泳用于解决相似条件的小分子量蛋白质,肽的债券PSPKC裂解的蛋白水解活动中ROS 17/2.8细胞溶解产物已经确定。Ser-Arg、Thr-Leu Ser-Val肽债券。日期,没有出现在蛋白水解活动描述了成骨细胞细胞溶解产物前面提到的肽键特异性,表明这些活动是小说。PSPKC-cleaved肽片段生成模式是类似的几个不同的成骨细胞的细胞溶菌产物。组织还可以打通PSPKC,但是肽片段产生的ROS 17/2.8模式在这些细胞lysatesappeared是独一无二的组织。

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