Human immunoglobulin

Human immunoglobulin preparations from pools of a great number of people (>1,000) with assumed antibodies against common viruses are used as a means of passive immunization in acute infections. More specific antibody preparations with high titers from patients who recovered recently from a viral disease or were immunized against toxins are also available in... 

The immune globulins are contraindicated in patients with a history of allergic reactions after administration of human immunoglobulin preparations and individuals with isolated immunoglobulin A (IgA) deficiency (individuals could have an anaphylactic reaction to subsequent administration of blood products that contain IgA). 

Processing of bacterial harvests Production of the viruses and the viral 4 Human immunoglobulins... 

Immunological products comprise a group of pharmaceutical preparations with diverse origins but with a common pharmacological purpose the enhancement of a recipienf s immune status in a manner that provides immunity to infectious disease. The immunological products that are generally available today are of three types vaccines, immunosera and human immunoglobulins. 

Immunosera, which were once very widely used in the prophylaxis and treatment of many infections, are little used today, as vaccines have made some immunosera unnecessary and lack of proven therapeutic benefit has caused others to be relegated to immunological history. Tetanus antitoxin is an exception in that it is a very effective prophylactic that is still used in countries where there are inadequate supplies of tetanus immunoglobulin. Human immunoglobulins have important but limited uses. 

Immunosera and human immunoglobulins depend for their protective effects on their content of antibodies derived, in the case of immunosera, flxm immunized animals and, in the case of immunoglobulins, flxm humans who have been immunized or who have high antibody titres consequent upon prior infection. This form of immunity, known as passive immunity, is achieved immediately but is limited in its duration to the time that protective levels of antibodies remain in the circulation see also Chapter 16. 

A feature that is common to vaccines, immunosera and human immunoglobulins is the maiked specificity of their actions. Each provides immunity to only one infection. This specificity has led to the development of vaccines and immunosera with several different components such as are present in the widely used diphtheria/tetanus/pertussis vaccines that are used to prevent the infectious diseases that commonly afflict infants and young children. 

Grabbe E.S., Buck R.P., Surface-enhanced Raman-spectroscopic investigation of human immunoglobulin-g adsorbed on a silver electrode, J. Am. Chem. Soc. 1989 111 8362-8366. 

Denizli, A., Rad, A.Y., and Piskin, E. (1995) Protein A immobilized polyhydroxyethylmethacrylate beads for affinity sorption of human immunoglobulin G./. Chromatogr. B. Biomed. Appl. 668(1), 13-19. June 9. 

T. Fonong and G.A. Rechnitz, Homogeneous potentiometric enzyme immunoassay for human immunoglobulin G. Anal. Chem. 56, 2586-2590 (1984). 

Recombinant DNA technology has provided an alternative (and successful) route of reducing the innate immunity of murine monoclonals. The genes for all human immunoglobulin sub-types have been cloned, and this has allowed generation of various hybrid antibody structures of reduced immunogenicity. 

Adalimumab (Humira) is a human immunoglobulin Gj monoclonal TNF-a antibody. The binding of adalimumab results in inactivation of the proinflammatory cytokine TNF-a. It is indicated for psoriatic arthritis and treatment of adults with moderate to severe chronic plaque psoriasis who are candidates for systemic therapy or phototherapy. The recommended dose for psoriatic arthritis is 40 mg subcutaneously every other week. The recommended dose for adults with plaque psoriasis is an initial dose of 80 mg, followed by 40 mg every other week starting 1 week after the initial dose. The most common adverse reactions are infections (e.g., upper respiratory, sinusitis), injection site reactions, headache, and rash. 

R. W. Nelson, D. Dogruel, and P. Williams. Mass Determination of Human Immunoglobulin IgM Using Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry. Rapid Commun. Mass Spectrom., 8(1994) 627-631. 

Recombinant Protein G from cell lysates of E. coli Semi-preparative purification Affinity (human immunoglobulin G) disks [74]... 

Three TNF antagonists are currently approved for the treatment of RA etaner-cept (ETN), infliximab (INF), and adalimumab. ETN a fusion protein of two identical chains of the recombinant human TNF receptor, p75, fused with the Fc portion of human immunoglobulin (Ig) G1 binds to soluble TNF-a in vivo. INF and adalimumab are both monoclonal antibodies to TNF-a INF is chimeric, and adalimumab is fully humanized. Both bind to soluble TNF-a, preventing TNF-a from binding to its receptors on cell surfaces. INF can also bind transmembrane TNF-a, fix complement, and cause cell lysis. 

If the antigen of interest is abundant and additional sensitivity is not required, then a two-step direct method, rather than a three-step indirect method, can be anployed. With the two-step method, the primary antibody is a biotin-labeled mouse monoclonal antibody, which is followed directly by the ABC incubation step. Because of the abundance of human immunoglobulins in tissue sections, methods for staining immunoglobulin often employ biotin-labeled mouse antihuman immunoglobulin reagents. 

K. Sato, M. Tokeshi, T. Odake, H. Kimura, T. Ooi, N. M. and T. Kitamori Integration of an Immunosorbent Assay System Analysis of Secretory Human Immunoglobulin a on Polystyrene Beads in a Microchip. Anal. Chem. 72, 1144 (2000). 

AMINO ACIDS, PEPTIDES PROTEINS Recommended nomenclature and symbolism for amino acids and peptides J. Biol Chem. (1985) 260, 14-42 Biochemistry (1975) 14, 449-462 Abbreviations and symbols for the description of the conformation of polypeptide chains /. Biol Chem. (1970) 245, 6489-6497 Nomenclature of iron-sulfur proteins Eur. J. Biochem. (1979) 93, 427-430 Corrections Eur. J. Biochem. (1979) 102, 315 Nomenclature of peptide hormones J. Biol Chem. (1975) 250, 3215-3216 Nomenclature of human immunoglobulins Eur. J. Biochem. (1974) 45, 5-6 Recommended nomenclature of glycoproteins, glyco-peptides, and peptidoglycans /. Biol Chem. (1987) 262, 13-18 Recommended nomenclature of electron-transfer proteins... 

Lefranc, M. R, Hammarstrom, L., Smith, C. I. E., and Lefranc, G., Gene deletions in the human immunoglobulin heavy chain constant region locus Molecular and immunological analysis. Immunol. Rev. 2, 265-281 (1991). 

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