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. Author manuscript; available in PMC: 2017 Apr 29.
Published in final edited form as: Biochem Biophys Res Commun. 2016 Mar 21;473(2):524–529. doi: 10.1016/j.bbrc.2016.03.096

Fig. 1.

Fig. 1

(A) The sequence of the expressed 1918 H1N1 NA contains seven potential N-glycosylation sites. Five sites (N-50 to 88) reside in one large tryptic peptide (6×His tag and S-37 to K-102, underlined) that is a part of the stalk region of the protein. The amino acid sequence numbering is according to GenBank AAF77036. (B) SDS-PAGE of the tetramer NA (T) and dimer NA (D), both reduced and alkylated. Bovine fetuin in native from and reduced/alkylated form was separated in the same gel as a resolution control. The form in reduced/alkylated was up-shifted, due to the carbamidomethylation of six pairs of disulfide bonds.