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Intravenous Immunoglobulin Therapy for Rheumatic Diseases

Shivashankar Othy, DVM, Michel D Kazatchkine, MD, Srini V Kaveri, DVM, PhD, and Jagadeesh Bayry, DVM, PhD

The immunoglobulins (Igs) are one of the major protein families found circulating in the blood. Igs are glycoproteins and are composed of two heavy and two light chains. Both chains are made up of variable and constant domains (Figure 1). The Igs recognize specific antigens through the fragment antigen-binding (Fab) region, whereas the fragment crystallizable (Fc) region interacts with Fc receptors and Fc-binding proteins such as complement. Igs are classified into five major isotypes based on their heavy chain constant domains: IgG, IgA, IgM, IgD, and IgE. Each Ig is made up of an identical pair of one of the two types of light chains: κ or λ. IgG is the most abundant Ig in the circulation and mediates the majority of antibody-based immunity against foreign antigens. IgG has a molecular weight of 150 kDa and exists in four different subclasses: IgG1, IgG2, IgG3, and IgG4.

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