Interheavy disulfide bridge in immunoglobulin G (IgG) reacting with dithionitrobenzoate

Reactive disulfide bonds in immunoglobulin G. A unique feature in serum proteins of different species

“…More recently this notion was examined in more detail using 14C-labelled NBSSBN [13]. At first, ES-values were determined by 24 hour incubations of serum samples of healthy humans, Sprague-Dawley rats and Swiss H:OF 1 mice with the radiolabelled reagent, followed by separation of the modified total IgG through Sephadex and measurement of the protein-bound radioactivity (cpm).…”

Directed immobilization of reduced antibody fragments onto a novel SAM on gold for myoglobin impedance immunosensing

“…In addition, the free-SH generated can be used to provide oriented immobilization with the antibody recognition site freely available. This should result in higher accessibility for antigens, less variable interaction kinetics, and thereby, improved analyte recognition [1,3,[6][7][8][9][10][11]. Amino-terminated SAMs are quite amenable to further modification and the heterobifunctional cross linker, succinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxyl (sulfo-SMCC) has been used to couple half-antibody fragments to an amine-terminated surface [3,[12][13][14][15].…”

Investigation of N-terminal glutamate cyclization of recombinant monoclonal antibody in formulation development

“…tions themselves but also on their locations [3][4][5][6][7][8][9][10]. Therefore, therapeutic mAbs also require extensive and stringent characterization of purity, structural integrity and stability.…”