Estudio de las lectinas presentes en el alga roja Tricleocarpa cylindrica

dc.contributorVega Castro, Nohora Angélica
dc.contributorPuyana Hegedus, Mónica
dc.contributorGrupo de Investigación en Proteinas Grip
dc.creatorDuarte Tayo, Angie Patricia
dc.date.accessioned2022-03-25T17:05:54Z
dc.date.available2022-03-25T17:05:54Z
dc.date.created2022-03-25T17:05:54Z
dc.date.issued2021
dc.identifierhttps://repositorio.unal.edu.co/handle/unal/81388
dc.identifierUniversidad Nacional de Colombia
dc.identifierRepositorio Institucional Universidad Nacional de Colombia
dc.identifierhttps://repositorio.unal.edu.co/
dc.description.abstractEl estudio en lectinas de algas es menor comparado con vegetales o animales, sin embargo, se han estudiado principalmente en algas rojas (Phylum Rhodophyta). Por otra parte, la purificación de estas moléculas es dispendiosa dada la cantidad de pigmentos que contienen sus extractos proteicos. En este estudio se llevaron a cabo ensayos de purificación de las lectinas del alga roja Tricleocarpa cylindrica, dado que previamente se detectó su actividad aglutinante; por otra parte, se ha reportado que estas lectinas tienen diferentes actividades biológicas que las postulan como moléculas de gran interés farmacológico. Inicialmente se realizó un tratamiento con acetona a la harina del alga para eliminar interferentes que producen hemólisis de eritrocitos, por precipitación con sulfato de amonio se detectó únicamente actividad aglutinante en la fracción del 50-80%s, los ensayos de inhibición con carbohidratos mostraron reconocimiento principalmente por D-glucosa. Aglutinó preferentemente eritrocitos de humano tipo B con cantidades de 0.6 g de proteína pura, similar a lo reportado para lectinas de otras especies de algas rojas. La lectina de Tricleocarpa cylindrica (LTC) se purificó con una combinación de métodos cromatográficos, que incluyeron intercambio iónico, afinidad y un paso final con HPLC. Esta nueva proteína se caracterizó por ser una glicoproteína con un peso molecular de 29 kDa por SDS PAGE, un punto isoeléctrico ácido (5.7) y alta estabilidad en un rango de pH de 3.0-7.4 y temperatura hasta los 58ºC. (Texto tomado de la fuente)
dc.description.abstractLectins from marine algae have not been studied such as vegetables or animals, even though, their study is centered in red algae (Phylum Rhodophyta). Furthermore, purification of these proteins is difficult due to pigments in saline extracts. In this study, purification of the lectins from the red algae Tricleocarpa cylindrica were carried out because hemagglutination activity was detected previously; additionally, these lectins could be molecules of great pharmacological potential for its various biological activities. First, removal of pigments was achieved by washing the algae flour with cool acetone to avoid hemolysis, precipitation assays from PBS extracts showed that the whole lectin was obtained in the fractions precipitated with ammonium sulphate 50-80%s. The lectin was able to agglutinate human RBCs from B and O donors; although it agglutinated preferentially B erythrocytes with a minimum lectin quantity of 0.6 g, like other species studied. Several purification procedures were assayed which included DEAE-sephadex, affinity chromatography, and the last step on HPLC. It led to obtaining a pure lectin having high specific agglutination activity (SAA). The PI showed a unique band at pH 5.7, in SDS-PAGE a band around 29 kDa, thermal stability (58 0C), and activity in the pH range 3.0-7.4.
dc.languagespa
dc.publisherUniversidad Nacional de Colombia
dc.publisherBogotá - Ciencias - Maestría en Ciencias - Bioquímica
dc.publisherDepartamento de Química
dc.publisherFacultad de Ciencias
dc.publisherBogotá, Colombia
dc.publisherUniversidad Nacional de Colombia - Sede Bogotá
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dc.rightsAtribución-NoComercial 4.0 Internacional
dc.rightshttp://creativecommons.org/licenses/by-nc/4.0/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleEstudio de las lectinas presentes en el alga roja Tricleocarpa cylindrica
dc.typeTrabajo de grado - Maestría


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