Monoclonal antibody IgG

Fig. 9. Conjoint Liquid Chromatography (CLC). Separation of proteins from mouse ascites and isolation of monoclonal antibody IgG in one step obtained by a combination of CIM QA and CIM Protein A Disks. Conditions Separation mode CLC (first disk CIM QA, 12 x 3 mm ID, 0.34 ml second disk - CIM Protein A, 12 x 3 mm ID, 0.34 ml, inserted in monolithic column housing) Instrumentation Gradient HPLC system with extra low dead volume mixing chamber Sample Mouse ascites Injection volume 20 pL Mobile Phase Buffer A 20 mM Tris-HCl, pH 7.4 Buffer B Buffer A + 1 M NaCl Buffer C 0.1 M Acetic acid Conditions Gradient 0 - 50 % B in 50 s, 100% A for 40 s, 100% C for 30 s Flow Rate 4 ml/min Detection UV at 280 nm... 

Several amperometric immunosensors have been developed for monoclonal antibodies (IgG), a-interferon and the pesticide 2,4-dichlorophenoxy-acetic acid (2,4-D) by using a flow-cell with the catching antibody covalently bound to a cellulose acetate or activated nylon membrane as shown in Fig. 3.31. B. With multiepitope antigens (e.g. a protein), after the antigen is bound and washed, a second enzyme-labelled antibody is used to form a sandwich... 

Figure 26-16 Purification of monoclonal antibody IgG by affinity chromatography on a 0.46 x 5 cm column containing protein A covalently attached to polymer support. Other proteins in the sample are eluted from 0 to 0.3 min at pH 7.6. When eluent pH is lowered to 2.6. IgG is freed from protein A and emerges from the column. [From B. J. Compton and L Kreilgaard. Chromatographic Analysis at Therapeutic Proteins," Anal. Chem. 1994,66, 1175A.]...

Figure 12.4 Schematic of a monoclonal antibody (IgG) and antibody fragment used in targeting drug debvery.

Direct, nonsurfactant-mediated immobilization of metallothionein proteins [207-209] and streptavidin [210] at MWCNTs has also been carried out, the hydro-phobic regions of the proteins probably being responsible for the adsorption. Specific affinity binding of proteins to unmodified SWCNT sidewalls was demonstrated by the adsorption of monoclonal antibodies, IgG, specific for C60 fuller-enes, in aqueous solution. The affinity binding originated from the structural similarity of the tube sidewall graphite network and the C(M fullerene [221]. It was shown that the specific binding site of the IgG antibody is a domain of hydrophobic amino acids. 

This review is intended to provide helpful information regarding potential monoclonal antibody IgG test article (non-CDR-mediated) binding to specific tissues, cell types or other tissue elements, and subcellular locations following exogenous intravenous administration in animal model test systems. Particulars specific to other routes of administration were reviewed by Lobo et al. [1]. 

Two monoclonal antibodies (IgG) were labeled with ferrocene, the first specific to histamine [30], a molecule implicated in allergic reactions, and the second specific to the hormone HCG [31], a glycoprotein biosynthesized by placental tissue throughout pregnancy. This procedure, involving a fraction of their lysine residues, is very similar to that used for triiodothyronine, except for the fact that activation of the ferrocenyl carboxylic acid 7 is achieved by reaction of EDAC and NHSS to give an intermediate N-sulfosuccinimidyl ester (Scheme 8.6). The number of Fc residues attached to the antibodies ranges from 4 to 11. 

Figure 31. Matrix-assisted laser desorption (MALDI) spectrum of a carefully purified monoclonal antibody (IgG of mouse against a specific human lymphokine)...

IgG below specified limit (if monoclonal antibodies used in purification) ELISA or RIA... 

The discovery of monoclonal antibodies and combining them with polymeric prodrugs is the newest approach to overcome the lack of selectivity for disposition in target tissue (23). Recently the selectivity of antibody-targeted polymeric anthracycline antibiotics to T lymphocytes was accomplished (25). In addition decreased immunogenicity of proteinaceous conjugates with IgG and human transferrin has been reported (26). 

Administration of Tyv-specific monoclonal antibodies to rat pups already infected with intestinal larvae causes larvae in the epithelium to be expelled (Carlisle et al, 1990). Only the LI stage is susceptible to expulsion once the larva has moulted to L2 it resists the effects of the antibodies (Carlisle et al, 1990). Expulsive immunity is transferred by three IgG isotypes, F(ab )2 fragments, as well as IgM (Carlisle et al., 1991a). These findings argue against a role for Fc-mediated effector functions and imply that antibodies against Tyv can disturb the larva s niche in a direct fashion. 

Bell, R.G., Appleton, J.A, Negrao-Correa, D.A. and Adams, L.S. (1992) Rapid expulsion of Trichinella spiralis in adult rats mediated by monoclonal antibodies of distinct IgG isotypes. Immunology 75, 520-527. 

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