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. 2019 Dec 10;39(12):BSR20191501. doi: 10.1042/BSR20191501

Figure 6. Experimental binding analysis of buffalo OVGP1 with different sugar ligands.

Figure 6

Fluorescence emission spectra of (AF) native OVGP1 and (GL) recombinant OVGP1 upon incubation with different concentrations of GlcNAc, GalNAc, Man, (GlcNAc)2, (GlcNAc)4 and (GlcNAc)6. Spectra for native and recombinant OVGP1 are shown in red. Spectra obtained at different concentrations of ligands i.e. 5, 10 and 15 mM are shown in pink, blue and green, respectively. (M) SDS–PAGE showing chitin-binding property of native OVGP1: lane 1 represents the purified proteins, lane 2 represents the protein molecular weight standard, lane 3 represents the bound fractions to chitin beads and lane 4 represents the unbound fractions after washing. (N) Western blot confirmation of chitin binding by native OVGP1 (lane 1: protein molecular weight standard, lane 2: bound fraction and lane 3: unbound fraction). (O) SDS–PAGE showing chitin-binding property of recombinant OVGP1: lane 1 represents the purified proteins, lane 2 represents the protein molecular weight standard, lane 3 represents the bound fractions to chitin beads and lane 4 represents the unbound fractions after washing. (P) Western blot confirmation of chitin binding by recombinant OVGP1 (lane 1: bound fraction, lane 2: unbound fraction and lane 3: protein molecular weight standard).