Zobrazeno 1 - 4
of 4
pro vyhledávání: '"J E, Labdon"'
Publikováno v:
Journal of Biological Chemistry. 268:8717-8726
AMP nucleosidase (EC 3.2.2.4) from Escherichia coli and AMP deaminase (EC 3.5.4.6) from bakers' yeast are proposed to regulate cellular AMP levels under allosteric control of the activator ATP and the inhibitor, PO4. Both enzymes contain catalytic si
Publikováno v:
The Journal of biological chemistry. 268(12)
AMP nucleosidase (EC 3.2.2.4) from Escherichia coli and AMP deaminase (EC 3.5.4.6) from bakers' yeast are proposed to regulate cellular AMP levels under allosteric control of the activator ATP and the inhibitor, PO4. Both enzymes contain catalytic si
Publikováno v:
The Journal of biological chemistry. 267(5)
p19 is a highly conserved 19-kDa cytosolic protein that undergoes phosphorylation in mammalian cells upon activation of several distinct signal transduction pathways. Its expression is widespread but developmentally regulated. To determine the in viv
Autor:
H V, Le, L, Ramanathan, J E, Labdon, C A, Mays-Ichinco, R, Syto, N, Arai, P, Hoy, Y, Takebe, T L, Nagabhushan, P P, Trotta
Publikováno v:
The Journal of biological chemistry. 263(22)
We have purified recombinant human interleukin 4 (huIL-4), formerly named B-cell stimulatory factor-1, from supernatants of COS-7 monkey kidney and L-929 cells transfected with the cDNA for huIL-4. The purified protein exhibited a specific activity o