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. Author manuscript; available in PMC: 2017 May 1.
Published in final edited form as: Free Radic Biol Med. 2016 Feb 16;94:145–156. doi: 10.1016/j.freeradbiomed.2016.02.012

Table 3.

Effect of mutation at L145 or/and L148 on the peroxidase and PLA2 activities of recombinant Prdx6 protein

Enzymatic activity nmol/min/mg protein
Peroxidase PLA2
WT 3900 ± 300 99.7 ± 3.5
L145E 1100 ± 100* (28%) 102 ± 4.7 (102%)
L148E 1300 ± 200* (33%) 98.5 ± 1.2 (99%)
L145/148E 300 ± 100*† (8%) 99.9 ± 0.9 (100%)

Peroxidase activity was measured at pH 7 using H2O2 as substrate; PLA2 activity was measured at pH 4 in the absence of calcium with [3H]-dipalmitoylphosphatidylcholine as substrate. πGST (equimolar to Prdx6) was added for peroxidase assay; GSH (5μM) was added for both assays. Values are mean ± SE for n=4. Numbers in parentheses indicate % of corresponding wild type (WT) value.

*

P<0.05 vs WT;

†

P<0.05 vs either single mutant protein.