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. 2016 Mar 2;3:15057. doi: 10.1038/mtm.2015.57

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Copyright © 2016 Official journal of the American Society of Gene & Cell Therapy

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Characterization of the heat stability and kinetic properties of HexM as compared to other Hex isozymes. (a) Protein stained SDS-PAGE gel demonstrating the purity of secreted HexM after Ni-NTA chromatography. The secreted, purified HexM precursor polypeptide (µ_p) versus the major mature α- and β- polypeptides (α_m, β_m) of isolated placental HexA. Molecular weight standards (Std) are shown at the right. (b) Confirmation was obtained using differential scanning fluorimetry that the β-subunit interface was successfully transferred into the HexM protein structure. The T_m of HexA calculated from its heat denaturation curve (solid line) was significantly lower (~10 °C) than those calculated for HexB (dotted line) and HexM (dashed line), which were virtually identical. (c,d) Comparison of the kinetics of purified HexM versus HexA for artificial substrates. The K_m and V_max values of HexM (open circles) and HexA (filled squares) for the MUG (c) and MUGS (d) substrates were determined from the specific activities of each isozyme (y-axis) at various concentrations of each substrate (x-axis) and fitted to the Michaelis-Menten equation using Prism Graphpad.