Sandbox324: Difference between revisions
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</ref>. This allows for the activity of the enzyme to be tracked by measuring the increase in absorbance over time. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a determined optimal pH of 6. Enzyme activity was measured via a change in absorbance at 405nm over 80 minutes. The data collected was consistent with that of hydrolases in other studies.<ref>Vázquez-Mayorga, E.; Díaz-Sánchez, Á.; Dagda, R.; Domínguez-Solís, C.; Dagda, R.; Coronado-Ramírez, C.; Martínez-Martínez, A. Novel Redox-Dependent Esterase Activity (EC 3.1.1.2) for DJ-1: Implications for Parkinson’s Disease. International Journal of Molecular Sciences 2016, 17 (8), 1346. https://doi.org/10.3390/ijms17081346. | </ref>. This allows for the activity of the enzyme to be tracked by measuring the increase in absorbance over time. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a determined optimal pH of 6. Enzyme activity was measured via a change in absorbance at 405nm over 80 minutes. The data collected was consistent with that of hydrolases in other studies.<ref>Vázquez-Mayorga, E.; Díaz-Sánchez, Á.; Dagda, R.; Domínguez-Solís, C.; Dagda, R.; Coronado-Ramírez, C.; Martínez-Martínez, A. Novel Redox-Dependent Esterase Activity (EC 3.1.1.2) for DJ-1: Implications for Parkinson’s Disease. International Journal of Molecular Sciences 2016, 17 (8), 1346. https://doi.org/10.3390/ijms17081346. | ||
</ref> | </ref> | ||
[[Image:Activity8.jpeg]] | [[Image:Activity8.jpeg]] | ||
