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The transformation frequency for the A. aculeatus uridine auxotroph tended to be lower than that of the wild type with the same AMT method (Table 6).
However, the N321H mutated enzyme was active over a broader pH range compared to the wild type, with no much change in the specific activity.
In XVM2 medium ΔXacFhaC adhered slightly less well than the wild type, with a 1.5 fold lower levels of CV stain retained (Figure 3A, right side).
For wild type cells about 5.4% were competent and values are given as % of wild type with standard deviation of two independent experiments.
Following sequence alignments of the wild type with the mutant, we found a C to G change in the At3g21200 gene of pgr7 (Figure 6B).
By comparing wild type with mutant huntingtin overexpressing striatal neurons, we addressed the question of the consequences of altered proteasome function.
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A truncated enzyme (XYL7-Tr3) acquired by protein engineering showed similar catalytic properties as the wild-type, with a tenfold increase in soluble protein yield by the mutant.
Transgenic plants were also more tolerant to Ca-deficiency conditions, although they showed no differences to wild-type with respect to overall Ca levels.
This reduction in efficiency is vastly increased, compared to the wild-type, with a dideoxynucleotide substrate.
The two discrepant cases were identified as mutant with the KRAS-TMGB test and initially as wild-type with sequencing.
Finally, the cepI mutant is less competitive than the wild-type, with a mean value of 0.42 for the CI.
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