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- W2022863611 abstract "In order to obtain a radioimmunoassay (RIA) technique for the measurement of human plasma myeloperoxidase (MPO), we purified the enzyme from polymorphonuclear granulocytes (neutrophils), and compared three methods of labeling it with125Iodine: chloramine T, lactoperoxidase, and an original technique of ‘self labeling’ based on the ability of the enzyme to oxidize and bind125I in the presence of H2O2. The chloramine T technique produced a degraded protein, as well shown by a high non-specific binding of tracer to antibody. The lactoperoxidase technique did not succeed in labeling MPO with an adequate specific activity. In contrast, the self-labeling method gave a stable tracer with a specific activity of 23 μCi/gmg MPO (85 MBq), a satisfactory level of immunoreactivity, and a low-specific binding (≤3%). After labeling, purification of tracer was achieved by gel filtration chromatography in phosphate buffer (0.05 M; pH7) to which 0.1% poly-L-lysine was added. The labeled molecule remained stable for 40 days and could be used for RIA with a polyclonal antibody raised in rabbits." @default.
- W2022863611 created "2016-06-24" @default.
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- W2022863611 date "1991-09-01" @default.
- W2022863611 modified "2023-09-23" @default.
- W2022863611 title "Self-labeling of human polymorphonuclear leucocyte myeloperoxidase with125iodine" @default.
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- W2022863611 doi "https://doi.org/10.1007/bf01929890" @default.
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