Effect of trifluoroethanol on the structure and activity of calf intestinal alkaline phosphatase

CHED 825

Joshua L. Schwartz, ecsuhai@transy.edu, Division of Natural Science and Mathematics, Transylvania University, 300 North Broadway, Lexington, KY 40508 and Eva Csuhai, ecsuhai@transy.edu, Division of Natural Sciences and Mathematics, Transylvania University, 300 North Broadway, Lexington, KY 40508.
We have studied the enzymology and protein structural implications of the interaction between calf intestinal alkaline phosphatase and various polar organic solvents. This enzyme had been previously reported to show activation in the presence of 2,2,2-trifluoroethanol a widely used protein structure altering chemical. We have looked at the effect of this solvent on enzyme activity to measure the Michaelis-Menten constant and the maximal rate of this enzyme in up to 30 % of trifluoroethanol. These changes were then compared to the changes experienced by a thermostable counterpart of this enzyme, alkaline phosphatase from Escherichia coli, studied by a fellow student. The implications of these activity changes are considered.
 

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

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008