ABSTRACT
En condiciones fisiológicas las células aeróbicas producen cantidades de Especies Reactivas de Oxígeno. La supervivencia celular depende del balance entre los procesos oxidativos y las defensas antioxidantes. Esta interacción determina si la célula se encuentra en estrés oxidativo o no. Recientes estudios sugieren que una reducida capacidad en el metabolismo oxidativo así como estados proinflamatorios contribuyen a cambios neurodegenerativos relacionados con la edad en los humanos. Por tal motivo en el presente estudio nosotros comparamos los niveles séricos de la actividad de la superóxido dismutasa (SOD), Catalasa (CAT) y también los niveles de malonildialdehido (MDA) y el factor de necrosis tumoral a (TNFa) en primates no humanos jóvenes y viejos. Nuestros resultados sugieren relación entre las alteraciones del metabolismo oxidativo con los cambios neurodegenerativos que ocurren en los monos.
Subject(s)
Animals , Aging/metabolism , Cell Survival/physiology , Haplorhini/metabolism , Superoxide Dismutase/physiology , Catalase/physiology , Cellular Senescence/physiology , Oxidative Stress/physiologyABSTRACT
A glycoprotein protein kinase was isolated from monkey cerebellum by polylysine-Sepharose chromatography and affinity chromatography on Sepharose 4B coupled to the lectin, Concanavalin A. The protein kinase phosphorylated casein on serine and threonine residues and was stimulated by polylysine, polyarginine, spermine, histone, protamine and sphingosine, but was inhibited by heparin, poly (Glu, Ala, Tyr) and poly (Glu, Tyr). These characteristics were typical of casein kinase II. The protein kinase also phosphorylated fibrinogen and calmodulin and exhibited similar characteristics of stimulation by polylysine or polyarginine. The phosphorylation of fibrinogen (a glycoprotein), but not casein or calmodulin (non-glycoproteins), was significantly inhibited by Concanavalin A. Unlike casein kinase II, the enzyme did not undergo autophosphorylation. The collective results suggested that the enzyme from monkey cerebellum was a casein kinase II-like protein kinase and that phosphorylation of a glycoprotein substrate (fibrinogen) by the kinase could be influenced by a carbohydrate binding lectin.
Subject(s)
Animals , Calmodulin/metabolism , Casein Kinase II , Caseins/metabolism , Cerebellum/enzymology , Fibrinogen/metabolism , Haplorhini/metabolism , Phosphorylation , Protein Serine-Threonine Kinases/metabolism , Substrate SpecificityABSTRACT
A detergent solubilised sucrase from monkey small intestine has been purified 388-fold to gel electrophoretic homogeneity with an overall recovery of 36%. The molecular weight of the enzyme was 263 kDa by gel filtration. Electrophoresis in the presence of SDS indicates that the enzyme is a hetero-dimer. Mixed substrate inhibition studies and inhibition by PCMB and Tris suggest the presence of two catalytically active sites in the form of maltase and sucrase with isomaltase activity being common to both sites. Polyclonal antiserum against the purified enzyme showed a single continuous precipitin line with the purified antigen.