Isolation, identification and Partial Purification of Lectin from Typhonium trilobatum
| Autor: | Niranjan Kumar Sana, Mrityunjoy Biswas |
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| Rok vydání: | 2014 |
| Předmět: | |
| Zdroj: | IOSR Journal of Pharmacy and Biological Sciences. 9:41-46 |
| ISSN: | 2278-3008 2319-7676 |
| DOI: | 10.9790/3008-09344146 |
| Popis: | In this investigation we included isolation, identification and partial purification and some characterizations of purified Lectin from Typhonium trilobatum. During the summer seasons, the rhizome of Typhonium trilobatum was collected from different sites of Rajshahi in Bangladesh and various steps were followed to isolate crude protein extract. For identification of protein, we used Hemaglutination activity assay and its agglutinated human (o +ve) blood cells. Lectin was purified by using DEAE-Cellulose column chromatography and UV Spectrophotometric method. During purity checking and molecular weight determination we used Gel Electrophoresis method and moved three bands. The molecular weight was calculated from the standard curve of reference proteins which was constructed by plotting molecular weight against relative mobility of the reference proteins on gel after electrophoresis and the molecular weight of the partial purified Lectin as determined by SDS-PAGE. It assumed that there were three Lectins present and estimated to be 19±1kDa, 40±1kDa and 90±1kDa of their molecular weights. The minimum concentration of Hemaglutination activity assay was 15.4μg/ml. These Lectins showed slight toxicity towards brine shirmp nauplii, the LC50 value was 9.90648. These Lectins also showed slight antibacterial activity against Escherichia coli (123 μg/disc and 184.8 μg/disc). We can develop techniques and knowledge of protein chemistry, molecular biology including genetic engineering, and structural biology including analysis for the structure-activity relationship and clarification for the mechanism of enzymatic reaction to promote the research. |
| Databáze: | OpenAIRE |
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