 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](wd5214fig2mag.jpg)
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Figure 2
Effect of pH on the stability of both TBNAT and MMNAT as measured using an enzymic assay. The enzymes were incubated prior to the assay at different pH values for 30 min in an ice bath. The intended pH levels were obtained by adjusting the pH of a combined buffer [100 mM equimolar mixture of MES (pKa 6.16), HEPES (pKa 7.55), Tricine (pKa 8.16) and CHES (pKa 9.55)] by one pH unit over the pH range 4–11 (note: pH values of 4 and 11 are not within the optimal buffer range). The activity of each enzyme was then measured at 297 K and pH 8 by the NAT activity assay in the presence of 500 µM HLZ. The reaction was performed in the linear range of the enzyme activity. The enzyme activities of each NAT are presented relative to the activity of that NAT at pH 8. Each point represents the mean ± standard deviation from triplicate determinations. The error bars are within the symbols. |
![[Figure 2]](wd5214fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
