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A Journal on Nuclear Medicine and Molecular Imaging
Affiliated to the and to the International Research Group of Immunoscintigraphy
Indexed/Abstracted in: Current Contents/Clinical Medicine, EMBASE, PubMed/MEDLINE, Science Citation Index (SciSearch), Scopus
Impact Factor 2,413
Online ISSN 1827-1936
Colcher D.*, Goel A., Pavlinkova G., Beresford G., Booth B., Batra S. K.
From the Department of Pathology and Microbiology [DC, AG, GP, GB, BB] and Department of Biochemistry and Molecular Biology [SKB] University of Nebraska Medical Center, Omaha, USA
Monoclonal antibodies (MAbs) may be considered ‘magic bullets’ due to their ability to recognize and eradicate malignant cells. MAbs, however, have practical limitations for their rapid application in the clinic. The structure of antibody molecules can be engineered to modify functional domains such as antigen-binding sites and/or effector functions. Advances in genetic engineering have provided rapid progress in the development of new immunoglobulin constructs of MAbs with defined research and therapeutic application. Recombinant antibody constructs are being engineered, such as human-mouse chimeric, domain-dispositioned, domain-deleted, humanized and single-chain Fv fragments. Genetically-engineered antibodies differ in size and rate of catabolism. Pharmacokinetic studies show that the intact IgG (150 kD), enzymatically derived fragments Fab’ (50 kD) and single chain Fv (28 kD) have different clearance rates. These antibody forms clear 50% from the blood pool in 2.1 days, 30 minutes and 10 minutes, respectively. Genetically-engineered antibodies make a new class of immunotherapeutic tracers for cancer treatment.