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Hormonal regulation of phosphorylase phosphatase activity in rat liver
Author(s) -
Farkas Ilona,
Tóth Béla,
Bot György,
Gergely Pál
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80753-0
Subject(s) - glycogen phosphorylase , glucagon , phosphorylase kinase , phosphatase , medicine , endocrinology , kinase , chemistry , protein kinase a , hormone , insulin , protein phosphatase 1 , alkaline phosphatase , phosphorylation , biochemistry , biology , enzyme
The effect of glucagon and insulin on rat liver phosphorylase phosphatase activity in vivo was investigated. The activity of phosphatase was found to decrease following the administration of glucagon and increase with insulin in a reversible manner. No change was detected in the activity of heat‐stable phosphatase inhibitors in the hormone‐treated samples. Liver protein kinases (regulatory subunit of cAMP‐dependent protein kinase and/or Ca 2+ ‐dependent phosphorylase kinase) are suggested to regulate the activity of hepatic phosphorylase phosphatase (type 1 and 2A).

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