Sentence examples for purified variants from inspiring English sources
Kinetic parameters (kcat and KM) were determined for WT and purified variants.
Fig. 5 shows wild-type mAOX1 with the purified variants on a native polyacrylamide gel, showing that all proteins had about the same purity.
The lower Moco content of the purified variants may be due to the modified purification protocol necessary for the purification of these mAOX1 variants, which did not bind to the benzamidine sepharose.
This observation suggested that the amount of heme associated with the purified variants also varied (Kery et al. 1994).
In vitro kinetics of purified variants showed that the process of directed evolution recovered proteolytic activity by an improvement in both ${k{{{\rm obs1}\hfill \atop 2\hfill}}}$2×10-foldld) and ${k{{{\rm obs2}\hfill \atop 2\hfill}}}$3×10-foldld) and also changed the burst amplitude, with diminishing improvements in later rounds.
Moreover, exposing the same gel to the affinity purified variant specific antibody obliterated this band also in the non-denaturing conditions (Figure 5C).
GC-MS analysis as performed for wild-type cADO indicated host-derived fatty acid ligands were not bound to the purified variant proteins.
To form a Rio2 Slx9 Ran Crm1 complex, GST-Rio2 variants were immobilized on GSH-Sepharose and incubated with buffer alone or 2µMM purified Slx9 variants for 1 hr at 4°C.Then, samples were incubated with 0.2 µM purified His6-RanQLGTP for 1 hr at 4°C.
To further probe the functional defects associated with these variants, we expressed and purified each variant for detailed structural and functional analyses.
The final purified protein variants were successfully immobilized on a biosensor chip and used in a surface plasmon resonance binding assay.
Electrochemistry was used to characterise the properties of these two engineered and purified hFMO3 variants followed by electrocatalysis experiments in the presence of three different hFMO3 substrates benzydamine, tamoxifen and sulindac sulfide.
