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New findings on SNP variants of human protein L-isoaspartyl methyltransferase that affect catalytic activity, thermal stability, and aggregation

Fig 3

Relative enzyme activities using 5 mg/ml bovine γ-globulin as the methyl acceptor.

Assays for each variant were carried out twice, each time in triplicate. Triplicates of the WT enzyme were always assayed in parallel with each variant to provide optimal normalization. Each data point (●) shown in the figure was normalized by dividing the 3H-methyl cpm obtained in that assay by the average of triplicate WT assays done in parallel. Red bars indicate the average of the variant data points. Although not always evident due to symbol overlap, there are six data points for each mutant, and 12 for the WT. In panel B, note the vertical scale is greatly amplified due to the very low activity of all three R36 variants.

Fig 3

doi: https://doi.org/10.1371/journal.pone.0198266.g003