Oxytocin inactivates and phosphorylates rat hepatocyte glycogen synthase
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منابع مشابه
Oxytocin inactivates and phosphorylates rat hepatocyte glycogen synthase.
Incubation of isolated rat hepatocytes with oxytocin produces a time- and dose-dependent inactivation of glycogen synthase. Such inactivation is associated with an increase in the phosphorylation state of the 88 kDa subunit of the enzyme, as observed after electrophoretic analysis of the 32P-labelled enzyme isolated by immunoprecipitation from cells incubated with [32P]phosphate. CNBr cleavage ...
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Vanadate inactivated rat hepatocyte glycogen synthase and activated glycogen phosphorylase in a dose- and time-dependent manner. These effects were observed in hepatocytes from both fasted as well as fed rats. When rat hepatocytes were preincubated with [32P]phosphate and then with vanadate, and the 32P-labeled glycogen synthase was specifically immunoprecipitated, it was observed that vanadate...
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Figure Legend: Figure 1 Glycogen accumulation–normal accumulation in hepatocytes in a female B6C3F1 mouse from a chronic study. Figure 2 Glycogen accumulation–normal mobilization of glycogen from centrilobular area in a male B6C3F1 mouse from a subchronic study. Figure 3 Glycogen accumulation–glycogen in all hepatocytes in a male B6C3F1 mouse from a subchronic study. Figure 4 Glycogen depletion...
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Thank you for submitting your manuscript for consideration to The EMBO Journal. I do apologize for the slight delay in getting back to you with a decision that was caused by one late incoming report. As you will see from the enclosed assessments, the referees appreciate the potentially interesting regulatory phosphorylation of AMPK by PKA. However, all three of them also request further delinea...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1989
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2610827