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La investigacion se ejecuto en la Finca Experimental “La Maria” propiedad de la Universidad Tecnica Estatal de Quevedo (UTEQ) localizada en el km 7 1 / 2 de la via Quevedo-Mocache; Provincia de Los Rios cuya ubicacion geografica de 1o 6’ 23” de latitud sur y 79o 29’ 12” de longitud oeste y a una altura de 73 msnm. El objetivo principal fue evaluar el comportamiento productivo con la inclusion del 20% de harinas arbustivas y arboreas tropicales. Se utilizaron 40 cuyes machos de 30 dias de edad. Se empleo un diseno completamente al azar con cinco tratamientos, cuatro replicas y la unidad experimental estuvo conformado por 2 cuyes. Para determinar las diferencias entre medias de tratamientos se aplico la prueba de Tukey (P≤0,05). Se evaluaron cinco tratamientos en dietas de: (T0) dieta 100% balanceado, (T1) 80% dieta y 20% harina de Morus alba , (T2) 80% dieta y 20% harina de Erythrina poeppigiana , (T3) 80% dieta y 20% harina de Tithonia diversifolia , (T4) 80% dieta y 20% harina de Hibiscus rosa-sinensis . Las variables bajo estudio fueron: Consumo de alimento de balanceado en materia seca g (CABMS), ganancia de peso g (GP), indice de conversion alimenticia (ICA) y rendimiento a la canal % (RC). La rentabilidad de los tratamientos se la determino a traves de la relacion beneficio-costo (R b/c). El mayor (P

The intracellular portion of the epidermal growth factor receptor consists of a tyrosine kinase domain of approximately 290 amino acids and a COOH-terminal regulatory domain of approximately 230 amino acids that contains five sites of autophosphorylation. The effect of autophosphorylation on the conformation of the intracellular domain has been analyzed using gel filtration. Both phosphorylated and dephosphorylated forms of the intracellular domain exist as monomers and as dimers and appear to have an extended conformation. The Stokes' radii of phosphorylated monomers and dimers were larger than those of the dephosphorylated forms, indicating that the dephosphorylated form is more compact. These results indicate that a significant conformational change occurs in the intracellular portion of the epidermal growth factor receptor upon tyrosine autophosphorylation.

Mammalian cells contain two subspecies of RNA polymerase II, designated IIO and IIA. The objectives of these studies were to determine the structural relationship between these subspecies and to determine the functional significance of these differences. Subunits IIo and IIa were purified from calf thymus, and the effect of alkaline phosphatase treatment on electrophoretic mobility and immunochemical reactivity was examined. The removal of phosphate converts subunit IIo to a form indistinguishable from that of subunit IIa. These results indicate that subunit IIo is produced by multisite phosphorylation of subunit IIa. The distribution of phosphate within subunit IIo was determined by CNBr cleavage of in vivo labeled HeLa cell RNA polymerase II. 32P-Labeled subunit IIo was purified by immunoprecipitation and cleaved with CNBr, and the resultant peptides were analyzed. The quantitative recovery of 32P in the C-terminal peptide establishes that this domain is the primary site of phosphorylation. In an effort to assess the level of phosphorylation of the transcriptionally active form of RNA polymerase II in HeLa nuclei, transcription was carried out in the presence of 4-thiouracil triphosphate and the nascent labeled transcript cross-linked to RNA polymerase. Specific photoaffinity labeling of subunit IIo was observed. Alkaline phosphatase treatment results in an increase in the mobility of photoaffinity labeled subunit IIo to approach that of subunit IIa. These results indicate that subunit IIo is a component of transcriptionally active RNA polymerase II.