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. , Besser , T. E. , Gay , C. C. , Davis , W. C. , Reeves , J.J. , McFadden , T. B. and Akers , R. M. ( 1999 ): Regulation of the immunoglobulin G1 receptor: effect of prolactin on in vivo expression of the bovine mammary immunoglobulin G1

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Garcia-Lloret, M., McGhee, S., Chatila, T. A.: Immunoglobulin replacement therapy in children. Immunol. Allergy Clin. North Am., 2008, 28 , 833

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Orvosi Hetilap
Authors: Levente Bodoki, Melinda Vincze, Zoltán Griger and Katalin Dankó

, S. V.: Mechanisms of action of intravenous immunoglobulins. Bull. Acad. Natl. Med., 2012, 196 , 39–47. [French] Kaveri S. V. Mechanisms of action of intravenous immunoglobulins

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References Aoki , T. , Honda , H. and Ishii , M. ( 2013 ): Immunologic profiles of peripheral blood leucocytes and serum immunoglobulin G in perinatal mares and

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Abstract  

Labeling of antibodies, immunoglobulin G (IgG), with a multitracer was investigated with the aim of its utilization in the preparation of radiopharmaceuticals. The labeling procedure consists of two steps: conjugation of diethylenetriaminepentaacetic acid (DTPA) cyclic dianhydride with IgG and subsequent labeling with the multitracer.

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)-positive lymphoproliferations in post-transplant patients show immunoglobulin V gene mutation patterns suggesting interference of EBV with normal B cell differentiation processes. Eur J Immunol 33 , 1593–1602 (2003). Brauninger A

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Journal of Radioanalytical and Nuclear Chemistry
Authors: C. Arteaga de Murphy, L. Meléndez-Alafort, O. Martínez-Rivero, E. Gómez and G. Ferro-Flores

Abstract  

A new technetium labeling method for immunoglobulin reduced with tris(2-carboxy-ethyl)phosphine hydrochloride is presented. The Sandoglobulina IgG source was assayed for purity and optimum reagent's concentration and incubation times were determined. It was purified by column chromatography and labelled with Sn2+ reduced technetium in the presence of MDP. The kit is easy to prepare, labeling efficiency is >(97±1.9) % and stable for 6 hours. The immunoreactivity of the99mTc-IgG was verified by electrophoresis and Western blot tests. The IgG retained its structure after both the reducing and labeling processes and it was the only labeled species.

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Abstract  

The aim of the study of labeling of ligand–antibody conjugates was to find optimal conditions of preparing of these conjugates and appropriate radioactivity of selected nuclide for applications in nuclear medicine. Conjugation of the γ-immunoglobulin G (human or bovine IgG, polyclonal antibodies) and bifunctional chelating agent, diethylenetriaminepentaacetic acid dianhydride (cDTPAA), was carried out. Various values of the cDTPAA/antibody ratio, the weight concentration of polyclonal or monoclonal antibodies (MEM-97) and buffers were used. Further, the labeling conditions of the DTPA–IgG conjugate by radionuclides 90Y and 177Lu were optimized, and the labeling yield and the conjugation ratio of prepared radionuclide–DTPA–IgG conjugates was determined. Optimal incubation time of the immunoglobulin conjugation was obtained at 30 min from mixing of individual components. The labeling yield of radionuclide–DTPA–antibody conjugate higher than 95% was achieved. Higher values of conjugation ratio of radionuclide–DTPA–antibody conjugate were achieved in 0.1 mol L−1 carbonate buffer, pH 8.5, and the 0.1 mol L−1 carbonate buffer is suitable for studied conjugation systems. This study showed that the labeling yield as well as the conjugation ratio of tested systems depend on the amount of antibody substance, bifunctional chelating agent/antibody molar ratio and pH value of the buffer used.

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99 103 Berta, A. and Lampé, Zs. (1998): Immunoglobulin levels in the tears of patients with corneal grafts and transplant rejection. Adv. Exp. Med. Biol. 438 , 603

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Abstract  

186Re has been regarded as a therapeutic radionuclide due to its favorable radition charecterstics. Procedures have been described to tag this radionuclide to bovine gamma-globulins as a model protein, by direct and indirect methods. The direct method employed glutathione (antioxidant) to reduce the disulfide moities of the protein (antibody). Thus in situ sulfhydryl groups are generated to provide groups for direct labeling with186Re in a lower valence state. For the indirect method186Re-DTPA is prepared and the186Re DTPA chelate is covalently coupled to the protein at room temperature using the carbodimide method. The products obtained by both the methods have been analyzed for radiochemical and immunological properties.

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