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The relative activity of purified mutants were also shown.
Two more fadR super-repressor mutants were also discussed.
Exemplary mutants were also produced and compared to native protein.
This cleavage was not an autocatalytic process since the E385/A mutants were also processed.
The deletion mutants were also able to associate with rom-1.
The other mutants were also considerably resistant to chemical oxidation than was the wild-type enzyme.
The catalytic capacities of other mutants were also lower than that of WT-hAS3MT.
AtBS14b knock-out mutants were also analyzed for BR dependent phenotypic expression, but no visible phenotypes were observed.
Both EC1118Δ519 and Mab2CΔ519 mutants were also less efficient to produce ethanol showing statistically significant lower values of glucose yield.
The enzyme activity results from the native and UV mutants were also supported by the zymogram analysis data.
The N-terminal octapeptide N8 and its mutants were also synthesized and tested for their potency as dimerization inhibitors.
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