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Effects of different ATP contents on phosphorylation level of glycogen phosphorylase and its activity in lamb during incubation at 4 ℃ in vitro
International Journal of Food Science & Technology ( IF 2.6 ) Pub Date : 2020-03-20 , DOI: 10.1111/ijfs.14565
Yuqiang Bai 1 , Xin Li 1 , Dequan Zhang 1 , Chengli Hou 1 , Xiaochun Zheng 1 , Li Chen 1 , Chi Ren 1
Affiliation  

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.

中文翻译:

不同ATP含量对4℃下体外培养羔羊糖原磷酸化酶磷酸化水平及其活性的影响

本研究的目的是研究ATP对4℃下体外培养期间羔羊糖原磷酸化酶活性的影响。。提取羊羔的肌浆蛋白并用不同含量的ATP处理,得到三组糖原磷酸化酶,分别具有低,中和高ATP含量组,每100μg蛋白的ATP量分别为0.5、2.0和2.5μM。对照组不添加ATP。结果表明,ATP促进了糖原磷酸化酶的磷酸化,而磷酸化修饰则促进了其活性。但是ATP抑制糖原磷酸化酶的活性,并且ATP优先参与磷酸化。当ATP浓度为每100μg蛋白0.5μM时,磷酸化修饰对糖原磷酸化酶活性的影响等于对ATP的抑制。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占主导地位。
更新日期:2020-03-20
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