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. Author manuscript; available in PMC: 2016 Oct 27.
Published in final edited form as: Adv Enzyme Res. 2014 Mar;2(1):39–48. doi: 10.4236/aer.2014.21004

Table 2.

Comparison of activity of PGH and CPG with reduced folates and PABA-GLU.

Substrate (10 µM) PGH (nmole/min/mg) PGH % CPG (nmole/min/mg) CPG %
PABA-GLU 0.145 + 0.0022 100 0.972 + 0.0035 100
5-formyl-tetrahydrofolate ND 0 1.49 + 0.00013 150%
5-methyl-tetrahydrofolate ND 0 4.47 + 0.00026 460%

Enzyme reactions were performed as described in the methods. Briefly, reaction mixtures consisted of 50 mM Tris, pH 7.3, substrate (10 µM) and divalent cation (1 mM MnCl2 for PGH and 1 mM ZnCl2 for CPG). Reactions were initiated with addition of enzyme, and the change in absorbance was monitored over time for 5 minutes. The initial rate was determined by linear regression analysis of data using Graph Pad Prism 5. Samples were done in triplicate. Data are reported as average ± standard deviation. ND means not detected.