Monoclonal antibodies against human thyroid stimulating hormone (hTSH) are among the key reagents required in the development of an immunoradiometric assay (IRMA) for hTSH in serum. In this study we have produced and characterized twelve hTSH monoclonal antibodies. Hybridomas were generated by fusion of B-lymphocytes from mice immunized with hTSH and myeloma cells. Clones producing antibodies against hTSH were selected using ELISA (Enzyme Linked Immunosorbent Assay). Antibodies from the selected and cloned hybridoma cells were purified by affinity chromatography and their reactivities were tested by ELISA against a panel of antigens, i.e., hTSH, bovine serum albumin (BSA), and milk protein, and also by studying the binding of these monoclonal antibodies with the radioiodinated antigens (hTSH, BSA, and milk protein). It was observed that some of the hTSH monoclonal antibodies produced were polyreactive, reacting with hTSH as well as with unrelated antigen BSA, while others were monoreactive, reacting only to hTSH.
Different monoclonal antibodies, both commercial and indigenously produced, were evaluated in various combinations to optimize an immunoradiometric assay (IRMA) system for human thyroid stimulating hormone (hTSH). During these studies, it was observed that mixing one of the indigenously produced hTSH monoclonal antibody (2B11) in the hTSH IRMA system using Immunotech (Beckman Coulter, Czech Republic) kit reagents, led to an overall increase in the assay binding and sensitivity (from 0.025 mIU/L to 0.015mIU/L) of this IRMA system. This is not a general property of all monoclonal antibodies against hTSH. The mechanism for this enhancement can be attributed to the formation of a multicomponent complex.
123I/131I labeled meta-iodobenzylguanidine (mIBG) is a radiopharmaceutical used for diagnosis of neuroendocrine tumors (NET) related to neural crest origin. Present work evaluates a newly synthesized 99mTc analogue of this radioiodinated derivative.
Radioimmunoassay (RIA) of human growth hormone (hGH) using lz51-1abeled tracer prepared from DNA recombinant hGH (r-hGH) and characterization of the tracer in the assay system are described. The radioiodination of r-hGH resulted in high yield of immunoreactive tracer. The immunoreactive fraction could be purified by geI-filtration on sephadex G-75. The quality of radioiodinated tracer of r-hGH has been found to be same as that of the tracer obtained from pituitary hGH (p-hGH) with respect to immunoreactivity, assay sensitivity and RIA standard curve parameters.
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