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dc.contributor.advisorUscian, John M.
dc.contributor.authorRodríguez-Muñoz, Adlin R.
dc.date.accessioned2018-08-09T14:35:19Z
dc.date.available2018-08-09T14:35:19Z
dc.date.issued2004
dc.identifier.urihttps://hdl.handle.net/20.500.11801/806
dc.description.abstractTrypsin is one of several animal digestive proteases whose activities collectively breakdown ingested proteins to facilitate gut amino acid absorption. The goals of this research were to purify and characterize trypsin from intestinal and pyloric caecal tissues of white grunt, Haemulon plumierii (Lacepède, 1801). Trypsin was purified 11-fold from intestinal and pyloric caecal tissues of the white grunt, through the sequential application of ammoniun sulfate fractionation, size exclusion chromatography, and affinity chromatography. The enzyme displayed optimal activity at pH 8 and 40 oC. It was completely inhibited by the presence of soybean trypsin inhibitor at a concentration of 100 %. SDS-PAGE analysis of the purified enzyme revealed a single band with an estimated molecular weight of 24 kDa. This white grunt trypsin was similar to those from other fishes in terms of its molecular weight, kinetic properties, and response to the presence of soybean Trypsin is one of several animal digestive proteases whose activities collectively breakdown ingested proteins to facilitate gut amino acid absorption. The goals of this research were to purify and characterize trypsin from intestinal and pyloric caecal tissues of white grunt, Haemulon plumierii (Lacepède, 1801). Trypsin was purified 11-fold from intestinal and pyloric caecal tissues of the white grunt, through the sequential application of ammoniun sulfate fractionation, size exclusion chromatography, and affinity chromatography. The enzyme displayed optimal activity at pH 8 and 40 oC. It was completely inhibited by the presence of soybean trypsin inhibitor at a concentration of 100 %. SDS-PAGE analysis of the purified enzyme revealed a single band with an estimated molecular weight of 24 kDa. This white grunt trypsin was similar to those from other fishes in terms of its molecular weight, kinetic properties, and response to the presence of soybean trypsin inhibitor.en_US
dc.description.abstractTripsina es una de las varias proteasas animales digestivas que rompen colectivamente las proteínas ingeridas, para facilitar la absorción de aminoácidos en el intestino. Las metas de esta investigación fueron purificar y caracterizar tripsina del tejido intestinal y ciego pilórico del pez cachicata, Haemulon plumierii (Lacepède, 1801) mediante la aplicación secuencial de fraccionamiento con sulfato de amonio, cromatografía de exclusión por tamaño y cromatografía de afinidad. La enzima desplegó actividad óptima a pH 8 y a 40 oC. Tripsina fue completamente inhibida por la presencia de inhibidor de tripsina de soya a concentración de 100 %. El análisis de SDS-PAGE de la enzima purificada reveló una banda con un peso molecular estimado de 24 kDa. Esta tripsina de cachicata fue similar a aquellas obtenidas de otros peces en términos de su peso molecular, propiedades cinéticas y respuesta a la presencia de inhibidor de tripsina de soya.en_US
dc.description.sponsorshipDepartment of Biology of the University of Puerto Rico-Mayagüez for financial support to complete this master’s thesisen_US
dc.language.isoenen_US
dc.subjectTrypsinen_US
dc.subjectAnimal digestive proteasesen_US
dc.subjectHaemulon plumierii (Lacepède, 1801)en_US
dc.subject.lcshTrypsinen_US
dc.subject.lcshGrunts (Fishes)--Molecular aspectsen_US
dc.subject.lcshTrypsin inhibitorsen_US
dc.titlePurification and kinetic characterization of trypsin from the intestine and pyloric caeca of the white grunt, Haemulon plumierii, (Lacepède, 1801)en_US
dc.typeThesisen_US
dc.rights.licenseAll rights reserveden_US
dc.rights.holder(c) 2004 Adlin R. Rodríguez-Muñozen_US
dc.contributor.committeeNavas, Vivian
dc.contributor.committeeBunkley-Williams, Lucy
dc.contributor.representativeKubaryk, John
thesis.degree.levelM.S.en_US
thesis.degree.disciplineBiologyen_US
dc.contributor.collegeCollege of Arts and Sciences - Sciencesen_US
dc.contributor.departmentDepartment of Biologyen_US
dc.description.graduationYear2004en_US


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