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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
Author(s) -
Bai Yuqiang,
Li Xin,
Zhang Dequan,
Hou Chengli,
Zheng Xiaochun,
Chen Li,
Ren Chi
Publication year - 2020
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.14565
Subject(s) - glycogen phosphorylase , glycogen , phosphorylation , incubation , phosphorylase kinase , glycogen synthase , glycogen branching enzyme , biochemistry , chemistry , adenosine triphosphate , biology
Abstract 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.