Figure 2: Biochemical and biophysical characterization of the prepared proteins.
From: Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion
(a) Size-exclusion analysis of nectin-1 (red), gD (blue) and the gD/nectin-1 complex (black). The chromatographs of the three prepared protein species on a calibrated Superdex 200 column (10/300 GL), as well as the separation profiles of each pooled samples (peaks 1, 2, 3 and 4) on SDS–PAGE, are shown. Clearly shown are that peak 3 has two proteins, gD and nectin-1; the shoulder peak, peak 1, has nectin-1 (dimer); and peak 2 has nectin-1 as well (monomer); peak 4 is gD. (b) The analytical ultracentrifugation profile of nectin-1 shows the sedimentation coefficient distribution analysis c(s). The two identified species, whose corresponding MWs were calculated to be 32 and 64 kDa, respectively, are indicated, demonstrating the monomer–dimer equilibrium for nectin-1 in solution.
