Zobrazeno 1 - 10
of 17
pro vyhledávání: '"G. A. Dunaway"'
Publikováno v:
Diabetes. 44:1285-1289
Publikováno v:
Laboratory animal science. 40(4)
We report that the short-term use of various anesthetic agents prior to decapitation causes alteration of the levels of fructose-2,6-bisphosphate in kidney, brain, heart, muscle, and liver. These data indicate that even light anesthesia can not be us
Purification and physiological role of a peptide stabilizing factor of rat liver phosphofructokinase
Autor:
G A Dunaway, H L Segal
Publikováno v:
Journal of Biological Chemistry. 251:2323-2329
A substance has been purified to apparent homogeneity from rat liver which, as previously reported (Dunaway, G. A., Jr., and Segal, H. L. (1974) Biochem. Biophys. Res. Commun. 56, 689-696), specifically stabilizes the major liver isozyme of phosphofr
Publikováno v:
Journal of Biological Chemistry. 253:7460-7463
Earlier work demonstrated that the activity of liver phosphofructokinase (PFK-L2) and immunoreactive PFK-L2 were decreased in diabetic rats and increased to normal or super-normal amounts following insulin treatment (Dunaway, G.A., and Weber, G., (19
Publikováno v:
Journal of Biological Chemistry. 256:7844-7848
Phosphofructokinase isozymes of fetal, neonatal, and adult rat heart and skeletal muscle were characterized by DEAE-cellulose chromatography, agarose gel electrophoresis, and immunodiffusion with specific antisera. The results of these studies indica
Autor:
G A Dunaway, T P Kasten
Publikováno v:
Journal of Biological Chemistry. 260:4180-4185
The complex nature of the brain 6-phosphofructo-1-kinase isozymes was examined by elution with a discontinuous gradient from QAE (quaternary aminoethyl)-Sephadex. In the first wash (150 mM NaCl), where the rat muscle 6-phosphofructo-1-kinase isozyme
Publikováno v:
Journal of Biological Chemistry. 261:7831-7833
Atrial 6-phosphofructo-1-kinase activity from the hearts of diabetic rats was decreased by 50%, but ventricular 6-phosphofructo-1-kinase activity was found not to be insulin-sensitive. This decrease in atrial 6-phosphofructo-1-kinase activity during
The 6-phosphofructo-1-kinase (PFK) subunits and isoenzymes were studied in human muscle, heart, brain, liver, platelets, fibroblasts, erythrocytes, placenta and umbilical cord. In each tissue, the subunit types in the native isoenzymes were character
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::290b86a5295018cefd5943a306c9c7e3
https://europepmc.org/articles/PMC1149058/
https://europepmc.org/articles/PMC1149058/
Autor:
G A, Dunaway, T P, Kasten
Publikováno v:
The Journal of biological chemistry. 260(7)
The complex nature of the brain 6-phosphofructo-1-kinase isozymes was examined by elution with a discontinuous gradient from QAE (quaternary aminoethyl)-Sephadex. In the first wash (150 mM NaCl), where the rat muscle 6-phosphofructo-1-kinase isozyme
Publikováno v:
The Journal of biological chemistry. 253(20)
Earlier work demonstrated that the activity of liver phosphofructokinase (PFK-L2) and immunoreactive PFK-L2 were decreased in diabetic rats and increased to normal or super-normal amounts following insulin treatment (Dunaway, G.A., and Weber, G., (19