Abstract
The pancreatic hormone, glucagon, stimulates the net uptake of inorganic (32)P in vivo into rat liver and its incorporation into proteins of microsomes, mitochondrial membranes, and lysosomes. Incorporation into cytosolic proteins was enhanced only slightly by glucagon. More than 95% of the protein-bound phosphate is present as phosphoserine. Both the radioactivity and the total amount of protein-bound phosphate are increased after injection of glucagon. Glucagon treatment enhanced (32)P incorporation into the alcohol-ether soluble lipids of mitochondria but did not alter the relative distribution of (32)P in various phospholipid species.
MeSH Terms
Amino Acids/analysis
Animals
Butyrates/pharmacology
Chromatography, Paper
Cyclic AMP/pharmacology
Fasting
Glucagon/pharmacology
Lipids/analysis
Liver/cytology
Lysosomes/analysis,metabolism
Male
Membranes/drug effects,metabolism
Mitochondria, Liver/analysis,metabolism
Oxidative Phosphorylation/drug effects
Phosphates/analysis
Phosphorus Isotopes
Protein Binding/drug effects
Rats
Time Factors
Chemicals
Amino Acids
Butyrates
Lipids
Phosphates
Phosphorus Isotopes
Glucagon
Cyclic AMP
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Zahlten R N
Hochberg A A
Stratman F W
Lardy H A
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