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. Author manuscript; available in PMC: 2020 Dec 14.
Published in final edited form as: Anal Biochem. 2020 Jan 23;598:113597. doi: 10.1016/j.ab.2020.113597

Fig. 5.

Fig. 5.

Biophysical characterization of purified NAMPT protein. (a) Mass spectrometry after purification of NAMPT protein. The purified protein has a molar mass cf 55.98 kDa representing the monomeric protein, and is equal within experimental error to the theoretically predicted molar mass of 55.5 kDa. (b) Circular dichroism spectrum of the purified protein after cleavage of the hexa-His-SUMO tag shows a characteristic secondary structure fold for purified NAMPT protein. (c) Dynamic light scattering (DLS) results of purified recombinant protein with and without DDM detergent. The NAMPT protein exists as higher order oligomers without DDM detergent and as monomer in presence of the detergent.