Isolation of Protein-Glycogen Complexes from Rat Skeletal Muscle in Acute Uremia: Role of Serine
| Autor: | Walter H. Hörl, August Heidland, R. M. Schäfer |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
medicine.medical_specialty
Phosphorylases chemistry.chemical_element Propranolol Calcium General Biochemistry Genetics and Molecular Biology Serine Glycogen phosphorylase chemistry.chemical_compound Internal medicine Glycogen branching enzyme medicine Animals Uremia biology Glycogen Proteins Skeletal muscle Rats Inbred Strains medicine.disease Diet Rats Glycogen Synthase medicine.anatomical_structure Endocrinology chemistry Acute Disease biology.protein Female Protein Binding medicine.drug |
| Zdroj: | Experimental Biology and Medicine. 169:519-526 |
| ISSN: | 1535-3699 1535-3702 |
| DOI: | 10.3181/00379727-169-41383 |
| Popis: | Attempts were made to isolate an intact protein–glycogen complex from rat skeletal muscle in acute and chronic uremia and after different treatment regimes. In control animals the amount of glycogen in the 30-pellet fraction was 16.5 mg and in rats with chronic uremia 27.6 mg. The yields of glycogen phosphorylase and synthetase do not correlate with the quantity of glycogen during isolation. In the presence of ATP, calcium, and magnesium, flash activation of phosphorylase was four to six times slower in rat than in rabbit muscle. In acute uremia, after feeding a mixed low-protein diet and Walser ketoacid mixture, a protein–glycogen complex could not be isolated. Additional administration of propranolol resulted in yields of only 10 and 7 μg glycogen after binephrectomy and ureter ligation, respectively. In contrast, glycogen concentration increased dramatically after sham operation (4.55 mg glycogen/mg protein). Additional administration of high doses of serine resulted in an increase of glycogen ... |
| Databáze: | OpenAIRE |
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