Zobrazeno 1 - 10
of 113
pro vyhledávání: '"T.H. Claus"'
Autor:
T.H. Claus, Daryl K. Granner
Publikováno v:
Diabetes. 45:110-111
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93f12e017a25854855b29119c3230f3a
https://doi.org/10.2337/diab.45.1.110
https://doi.org/10.2337/diab.45.1.110
Autor:
T.H. Claus, J.D. Bloom
Publikováno v:
Drugs of the Future. 19:23
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd4cf822aab38d5e46f6f48ca232392b
https://doi.org/10.1358/dof.1994.019.01.235296
https://doi.org/10.1358/dof.1994.019.01.235296
Autor:
Pamela S. Keim, Donald F. Steiner, T.H. Claus, Robert L. Heinrikson, Simon J. Pilkis, B Coven, M R El-Maghrabi, H S Tager
Publikováno v:
Journal of Biological Chemistry. 255:2770-2775
Fructose-1,6-bisphosphatase from rat liver was phosphorylated with cyclic AMP-dependent protein kinase and [gamma-32P]ATP. Brief exposure of the 32P-labeled enzyme to trypsin removed all radioactivity from the enzyme core and produced a single-labele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61fefa46775c1cafb4fbac36a0df0400
https://doi.org/10.1016/s0021-9258(19)85805-2
https://doi.org/10.1016/s0021-9258(19)85805-2
Publikováno v:
Journal of Biological Chemistry. 251:7841-7852
The hormonal control of [14C]glucose synthesis from [U-14C-A1dihydroxyacetone was studied in hepatocytes from fed and starved rats. In cells from fed rats, glucagon lowered the concentration of substrate giving half-half-maximal rates of incorporatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::381b104b785b04e0e840e33d1bdc407c
https://doi.org/10.1016/s0021-9258(19)57012-0
https://doi.org/10.1016/s0021-9258(19)57012-0
Publikováno v:
Journal of Biological Chemistry. 255:668-675
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80a29077e93a64284ebd0638742ba86b
https://doi.org/10.1016/s0021-9258(19)86229-4
https://doi.org/10.1016/s0021-9258(19)86229-4
Publikováno v:
Journal of Biological Chemistry. 257:7541-7548
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccc017fc266dbd04ff7506302aac3d2c
https://doi.org/10.1016/s0021-9258(18)34413-2
https://doi.org/10.1016/s0021-9258(18)34413-2
Publikováno v:
Journal of Biological Chemistry. 256:3619-3622
Rat liver fructose-1,6-bisphosphatase, which was assayed by measuring the release of 32P from fructose 1,6-[1-32P]bisphosphate at pH 7.5, exhibited hyperbolic kinetics with regard to its substrate. beta-D-Fructose 2,6-bisphosphate, an activator of he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9181671b5058afcc4601138c7f63267a
https://doi.org/10.1016/s0021-9258(19)69494-9
https://doi.org/10.1016/s0021-9258(19)69494-9
Publikováno v:
Journal of Biological Chemistry. 254:7855-7864
The regulation of pyruvate kinase in isolated hepatocytes from fasted rats was studied where the intracellular level of fructose 1,6-bisphosphate was elevated 5-fold by the addition of 5 mM dihydroxyacetone. In this case, flux through pyruvate kinase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9044408fda7b8acfcc8987bc0323a945
https://doi.org/10.1016/s0021-9258(18)36025-3
https://doi.org/10.1016/s0021-9258(18)36025-3
Publikováno v:
Proceedings of the National Academy of Sciences. 77:6501-6505
Addition of glucagon to isolated hepatocytes reduced the activity of 6-phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) and pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40). Phosphorylation contribu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8aa936dfb845548271372b42249f0c9e
https://doi.org/10.1073/pnas.77.11.6501
https://doi.org/10.1073/pnas.77.11.6501
Publikováno v:
Journal of Biological Chemistry. 257:7603-7607
An enzyme activity that catalyzes the hydrolysis of phosphate from the C-2 position of fructose 2,6-bisphosphate has been detected in rat liver cytoplasm. The S0.5 for fructose 2,6-bisphosphate was about 15 microM and the enzyme was inhibited by fruc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1c6d387e1062866225d888da11a4b3fd
https://doi.org/10.1016/s0021-9258(18)34422-3
https://doi.org/10.1016/s0021-9258(18)34422-3