Effects of different ATP contents on phosphorylation level of glycogen phosphorylase and its activity in lamb during incubation at 4 C in vitro

Effects of different ATP contents on phosphorylation level of glycogen phosphorylase and its activity in lamb during incubation at 4 C in vitro
复制标题

不同ATP含量对4℃体外培养羔羊糖原磷酸化酶磷酸化水平及其活性的影响

DOI:
10.1111/ijfs.14565
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发表时间:
2020
影响因子:
3.3
通讯作者:
Chi Ren
Chi Ren
中科院分区:
农林科学3区
文献类型:
--
作者:
Yuqiang Bai;Xin Li;Dequan Zhang;Chengli Hou;Xiaochun Zheng;Li Chen;Chi Ren

文献摘要

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本研究旨在探讨ATP对体外培养4℃羔羊糖原磷酸化酶活性的影响。提取羔羊肌浆蛋白,用不同含量的ATP进行处理,得到三组糖原磷酸化酶,ATP含量分别为0.5、2.0和2.5 μM / 100 μg蛋白。对照组不添加ATP。结果表明,ATP促进糖原磷酸化酶的磷酸化,磷酸化修饰促进糖原磷酸化酶的活性。而ATP抑制糖原磷酸化酶的活性,优先参与糖原磷酸化。当ATP浓度为0.5 μM / 100 μg蛋白时,磷酸化修饰对糖原磷酸化酶活性的影响相当于对ATP的抑制作用。随着孵育时间的延长,糖原磷酸化酶磷酸化对其活性的影响逐渐成为主导。
The aim of this study was to investigate the effects of ATP on glycogen phosphorylase activity in lamb during incubation at 4℃in vitro. Sarcoplasmic proteins from lamb were extracted and treated with different contents of ATP to get three groups of glycogen phosphorylase with low, middle and high ATP content groups, the amount of ATP were 0.5, 2.0 and 2.5 μM per 100 μg protein, respectively. The control group was without ATP adding. The results showed that ATP promoted the phosphorylation of glycogen phosphorylase, and phosphorylation modification promoted its activity. But ATP inhibited the activity of glycogen phosphorylase and ATP preferentially participated in phosphorylation. When ATP concentration was 0.5 μM per 100 μg protein, the effect of phosphorylation modification on the activity of glycogen phosphorylase was equal to the inhibition of ATP. The effect of glycogen phosphorylase phosphorylation on its activity gradually became dominant as incubation time prolonged.