Journal: PLoS ONE
Article Title: Differential thermal stability, conformational stability and unfolding behavior of Eis proteins from Mycobacterium smegmatis and Mycobacterium tuberculosis
Figure Lengend Snippet: Time kinetics, temperature stability and steady-state kinetic parameters of KAN acetylation by MsEis and RvEis. Time course of changes in the absorbance at 412 nm of NTB - ions formed as a result of acetyltransferase activity of MsEis and RvEis proteins (Panel A) . The effect of temperature on the catalytic activity of MsEis and RvEis was determined after incubating the Eis proteins at different temperatures ranging from 20°C to 80°C (Panel B) . Kinetic parameters were calculated for the acetylation of KAN by MsEis and RvEis at fixed concentration of acetyl CoA and increasing concentration of KAN antibiotic (Panel C) . The experimental values were fitted to Michaelis-Menten equation using OriginPro 8.0 software (Origin Labs, Northampton, USA).
Article Snippet: The obtained data points were fitted to three-state model (biDose-response curve of nonlinear regression analysis) using OriginPro 8 software (Origin Lab, Northampton, USA).
Techniques: Activity Assay, Impedance Spectroscopy, Concentration Assay, Software