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Leishmaniasis is an infectious disease caused by parasitic protozoans of the genus Leishmania. A potential target for drug design and treatment development for leishmaniasis is the enzyme Secreted Acid Phosphatase (SAP). This undergraduate research attempted to partially purify SAP from Leishmania tarentolae using ion exchange chromatography (Whatman DE51 and CM- Sephadex) and affinity chromatography (Con-A Sepharose 4B). The effectiveness of purification was evaluated via UV/Vis spectroscopy and polyacrylamide gel electrophoresis (PAGE) was used to estimate the molecular weight of SAP. The enzyme activity presented in each column fraction was detected by using p-nitrophenylphosphate (pNPP) as artificial substrate and monitoring product formed at 405 nm. At this time, only a little enzyme activity was retained in the columns. Adjusting the column length, the concentration and the pH of the elution solution might increase the amount of enzyme being retained. Analyzing the column flow-through fractions by PAGE resulted in two protein bands at approximately 28 and 62.5 kDa. However, a Brain Heart Infusion (BHI) medium control must be analyzed to confirm whether these protein bands were of the medium background or of SAP.
Lai, Quyen, "PURIFICATION OF SECRETED ACID PHOSPHATASE FROM LEISHMANIA TARENTOLAE" (2022). University Research Symposium. 383.