985 resultados para PAK FA


Relevância:

20.00% 20.00%

Publicador:

Resumo:

Nº 422 del catálogo Fons de Teatre Valencià de la Biblioteca Bas Carbonell

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Notificación a los jurados y universidad de Covet de las 4 libras y 1 hombre en el repartimiento que les ha correspondido del Consell del Batalló

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Nella sua "dichiarazione di poetica", Alberto Campo Baeza confessa che la cosa che più gli sta a cuore è la bellezza, che persegue con le armi della ragione e dell'immaginazione, confortato dalle parole di illustri predecessori, come Cervantes e Goya, Platone e Sant'Agostino, Vitruvio e Keats

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Hay un ejemplar encuadernado con: Romans, y coloqui nou, pera divertir el humor y desterrar la melancolia, yà que no tenim dinès ... (NP849.91/3085).

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Hay un ejemplar encuadernado con: Poesías colocadas en el pórtico del Convento de San Francisco de Valencia (NP849.91/3086).

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Hay un ejemplar encuadernado con: Romans, y coloqui nou, pera divertir el humor y desterrar la melancolia, yà que no tenim dinès ... (NP849.91/3085).

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Myosin I heavy chain kinase from Acanthamoeba castellanii is activated in vitro by autophosphorylation (8–10 mol of P per mol). The catalytically active C-terminal domain produced by trypsin cleavage of the phosphorylated kinase contains 2–3 mol of P per mol. However, the catalytic domain expressed in a baculovirus–insect cell system is fully active as isolated without autophosphorylation in vitro. We now show that the expressed catalytic domain is inactivated by incubation with acid phosphatase and regains activity upon autophosphorylation. The state of phosphorylation of all of the hydroxyamino acids in the catalytic domain were determined by mass spectrometry of unfractionated protease digests. Ser-627 was phosphorylated in the active, expressed catalytic domain, lost its phosphate when the protein was incubated with phosphatase, and was rephosphorylated when the dephosphorylated protein was incubated with ATP. No other residue was significantly phosphorylated in any of the three samples. Thus, phosphorylation of Ser-627, which is in the same position as the Ser and Thr residues that are phosphorylated in many other kinases, is necessary and sufficient for full activity of the catalytic domain. Ser-627 is also phosphorylated when full-length, native kinase is activated by autophosphorylation.