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Updated: Jul 30, 2026

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
Published on: October 23, 2018
The short term hormonal control of cytoplasmic protein phosphorylation in hepatocytes from fed rats
Abstract:
Exposure of 32P-prelabelled isolated hepatocytes to vasopressin affected the phosphorylation of nine of the 26 phosphoproteins resolved by sodium dodecyl sulphate gel electrophoresis. Glucagon (2 nM) or cyclic AMP elicited significant changes in the phosphorylation of only four phosphoproteins. A very high concentration of glucagon (1000 nM) affected additional phosphoproteins. Insulin alone significantly increased the phosphorylation of a single protein. Vasopressin, A23187, glucagon and cyclic AMP all induced the dephosphorylation of a single phosphoprotein of mol. wt 20,000. The significance of these results with respect to the short-term control of hepatic metabolism is discussed.
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