Document Type
Honors Project
First Advisor
Dr. Joseph Crockett
Degree Award Date
Spring 2000
Keywords
Cation Size, Inhibition, Acid Phosphatase
Disciplines
Analytical Chemistry | Chemistry | Laboratory and Basic Science Research
Abstract
The effect of cation size on the enzymatic reaction of acid phosphatase with PNPP was further examined using the Hanes transformation of the Michaelis-Menten equation of enzyme kinetics. A series of six divalent metals (M2+) - barium, cadmium, calcium, cobalt, copper, and strontium as nitrate salts - were tested using this method to obtain the values of KM and V max for the reaction when the metal was present in the reaction mixture. The difference between the value of V max for the inhibited reaction and the value when not inhibited yielded how the metal affected the reaction's velocity. Data obtained showed that there was little effect of ion radius on V max, and virtually no affect of the radius on KM. There is, however, a decreasing trend of binding affinity as cationic radius increases. Future studies will look at the affect other cations and anions in terms of differing charge and structure.
Recommended Citation
Cash, Philip, "Effect of Cation Size on the Inhibition of Acid Phosphatase" (2000). Honors Projects. 462.
https://digitalcommons.bridgewater.edu/honors_projects/462