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The T. gondii enzyme differs from other tyrosine hydroxylases in its catalytic efficiency with both substrates and is, hence, bifunctional.
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Later, the two substrates were well aligned under a microscope with the assistance of markers on both substrates and were eventually brought into contact to form permanent bonding.
The activity of the individual enzymes was tested on both substrates and was compared to that of the combined enzymatic activity in order to determine the apparent synergy between them (Additional file 4: Table S2).
hFEN1 was very active on both substrates, and hEXO1 was inactive (Fig. 3B, C).
Taken together, our results suggest that both substrates and ABPs are viable tools for imaging protease activity using non-invasive imaging methods.
Under these conditions, ALP activity greatly increased in both substrates and levels were higher in 3D than in 2D surfaces (Fig. 1D).
Specifically, the addition of TGF-β1 was able to reduce PDGF-BB-stimulated migration and proliferation of rVSMC on both ECM substrates and was also able to restore PDGF-BB-stimulated reductions in VSMC adhesion on these ECM.
Both proteins are known to bind partly the same substrates and are both expressed in the brain [19,22,34].
Selection of both substrate and strain are critical to ensure a targeted substrate conversion to the final product, be it in the conversion of oligosaccharides by Lactobacillus spp.
Complex interactions of the C-terminus with both substrate and product were observed via a specifically designed tryptophan sensor, suitable for further detailed kinetic and ligand binding studies.
SERS spectrum for Nd2O3 was investigated for both substrates, and a satisfactory enhancement was observed.
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