• 主页
  • 查找结果
  • Calpastatin inhibits the activity of phosphorylated μ-calpain in vitro.

Calpastatin inhibits the activity of phosphorylated μ-calpain in vitro.

Food chemistry (2018-10-31)
Manting Du, Xin Li, Zheng Li, Qingwu Shen, Chi Ren, Dequan Zhang
摘要

The objective of this study was to investigate the effect of phosphorylation on the sensitivity of μ-calpain to the inhibition induced by calpastatin. Purified μ-calpain was incubated with alkaline phosphatase (AP) or protein kinase A (PKA) to modulate the phosphorylation level of μ-calpain. Accurately 25, 50, 100 and 150 units of AP/PKA-treated μ-calpain were mixed with the same amounts of heat stable proteins and incubated at 4 °C. In the calpastatin-free system, AP and PKA-treated μ-calpain had higher proteolytic activity compared to the control. Intact AP-treated μ-calpain degraded fastest in the 50, 100 and 150 unit μ-calpain incubation systems. However, the degradation rate of μ-calpain in control and PKA group was non-significant in 100 and 150 unit μ-calpain systems. Our results demonstrated that, compared to dephosphorylated and control μ-calpain, calpastatin presents greater inhibition to PKA phosphorylated μ-calpain. This study increases understanding of the mechanism of μ-calpain activity regulated by phosphorylation.

材料
货号
品牌
产品描述

Sigma-Aldrich
单克隆抗-钙抑素 小鼠抗, clone 1F7E3D10, ascites fluid, buffered aqueous solution

社交媒体

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

Merck

科研、开发、生产。

作为生命科学行业的全球领先供应商,我们致力于为科研、生物技术开发和生产,以及制药药物疗法开发和生产提供各类解决方案和服务。

© 2021年版权归德国达姆施塔特默克集团(Merck KGaA)及/或其附属公司所有。版权所有。

未经许可,严禁复制本网站上的任何资料。