Tübingen, Univ., Diss., 2007.

El presente proyecto determina la viabilidad técnica económica para la instalación de un criadero de caracoles comestibles terrestres de la especie HELIX ASPERSA, para su comercialización en el extranjero en su forma precocida y congelada sin concha. El mercado objetivo se conforma por las casas importadoras de Madrid, las cuales adquieren caracoles precocidos y congelados para destinarlos a compradores que exigen carne de caracol de calidad y un abastecimiento constante y creciente. El criadero de caracoles comestibles terrestres se establecerá en el Departamento de Lima, en la Provincia de Lima y en el Distrito de Punta Negra, principalmente por las facilidad de acceso y cercanía a puertos e insumos. El proyecto tiene una vida útil de siete años y planea la producción de 26 TM por año de carne de caracol precocida congelada, para ello durante el primer año de operaciones se alcanzará 15.7 TM cantidad con la que abastecerá el 5.5% del mercado meta y desde el segundo año hasta el año siete 26 TM promedio por año con un 8% en promedio de participación en el mercado. La inversión total asciende a 180369 dólares, los inversionistas aportarán el 65% de la inversión total, alcanzando una suma de 117240 dólares. El 35% restante de la inversión total es 63129 dólares y se obtendrá mediante un préstamo solicitado a la banca comercial. Para el desarrollo del proyecto se utiliza una tasa de descuento de 12%, con dicha tasa de descuento se tiene un VANE = 244801 dólares y un VANF = 243026 dólares; una TIRE = 38% y una TIRF = 45%; se presenta el fenómeno del apalancamiento financiero; y el PRI es 3 años; estos indicadores de rentabilidad permiten concluir que la realización del proyecto es viable desde el punto de vista económico y financiero. Se concluye que dadas las condiciones esenciales para el desarrollo del presente proyecto, la ejecución del proyecto es viable tecnológica y económicamente. / Tesis

published_or_final_version / abstract / Anatomy / Doctoral / Doctor of Philosophy

No description available.

CPF1 (<strong>c</strong>entromere <strong>p</strong>romoter <strong>f</strong>actor 1) of Saccharomyces cerevisiae is a multifunctional protein. This multifunctionality may be associated with the different forms of the protein. To date, no clear function has been attributed to this protein. The general roles currently attributed to CPF1 are: maintenance of proper chromosome segregation or centromere function; methionine prototrophy and chromatin modulation. A series of recent papers have suggested the possibility of CPF1 being involved in protein-protein interactions. This thesis shows that CPF1 has an additional protein-protein interaction domain which is a coiled-coil. A truncation of CPF1 coding for only the C-terminal dimerization motif was cloned into a 17 expression vector and the protein, Dd, was produced in and purified from E. coli. Characterisation of the conformation of the C-terminal dimerization domain of CPF1 show the presence of a leucine zipper in Dd and that Dd forms a dimer under physiological conditions. Sequence alignment analysis of CPF1 and other bHLHZIP proteins identified a conserved serine residue in the basic domain of CPF1 and a conserved asparagine residue in the leucine zipper. Point mutations were introduced separately mutating these residues into either alanine or glutamate. The mutant alleles were cloned into yeast expression vectors. The cloned alleles were used to transform YAG93, a cpf1 deletion strain. Characterisation of the transformants obtained indicate the possibility of CPF1 being involved in the spindle assembly checkpoint control, possibly as a tethering protein. Finally, attempts were made to identify interacting partners of CPF1 and a purification scheme was designed to purify a putative CPF1 complex. Initially, a GST-CPF1 chimera was used to screen radioactively labelled crude yeast extracts for interacting partners of CPF1. This strategy identified five or six potential proteins which might form a multiprotein complex with CPFl. Attempts were then made to purify this putative complex from S. cerevisiae. The partially purified extracts were tested for CDEI activity, indicative of the presence of CPF1 in the samples and. tjhen analysed for protein content. The samples were also tested in a Holiday junction binding assay and in a histone acetyltransferase activity assay. In conclusion, CPF1 is a bHLHZIP protein that has a role in nutrient signalling and checkpoint control, possibly by acting as an intermediary protein that recruits essential factors to gene promoters or the centromere by protein-protein interactions.

Thesis (Ph.D.)--University of Melbourne, Howard Florey Institute of Experimental Physiology and Medicine and Dept. of Anatomy and Cell Biology, 2003. / Typescript (photocopy). Includes bibliographical references (leaves 108-130).

Thesis (Ph. D.)--University of Hong Kong, 2008. / Also available in print.

Thesis (Ph. D.)--University of Hong Kong, 2008. / Also available online.

Universiẗat, Diss., 2003--Köln.

No description available.