CHED 786 |
| We have studied the enzymology and protein structural implications of the interaction between the thermostable Escherichia coli alkaline phosphatase and its surrounding buffer solution. This enzyme has a unique feature: it had been previously reported to show increased activity in the presence of 2,2,2-trifluoroethanol at high substrate concentrations in the presence of a carbonate buffer solution at pH 10. This activation was not observed in Tris buffer, at pH 8.0. We have looked at the effect of the buffer ions versus general ionic effects in solution on enzyme activity by measuring the Michaelis-Menten constant and the maximal rate of this enzyme at different pH values of both the carbonate and Tris solutions, with pH 9.0 as the overlap between the two conditions. We have also studied the effect of temperature on the enzyme activation. The implications of these activity changes are considered with regards to buffer-protein interactions. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |