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• W1521360157 abstract "An IgA class monoclonal antibody (2:2 G:5) to tissue plasminogen activator (t-PA) was raised by standard immunisation and cloning procedures. It was purified from ascites using ammonium sulfate precipitation, Sepharose-protein A chromatography, Sepharose-lysine treatment, DEAE Affi-Blue ion exchange chromatography and affinity chromatography on Sepharose-t-PA. After purification, the existence of free light and heavy chains and light—chain dimers, under denaturing but non-reducing conditions, indicated that the antibody preparation contained IgA type 2. The antibody inhibited t-PA mediated plasminogen activation but not amidolytic activity on low molecular weight chromogenic substrates. The antibody precipitated t-PA both in agarose double-diffusion and in solution. This suggests that t-PA may have two similar epitopes, and these are likely to be situated in the kringle regions. Kringle-binding ligands, e.g. arginine, inhibits the precipitation reaction, with half-maximal inhibition at 100 mmol. At this concentration of arginine, one-chain t-PA is also dissociated from fibrin, evidenced by a decrease in the fibrin-caused stimulation of amidolytic activity. Thus, the antibody might be used to study the fibrin binding of tissue plasminogen activator." @default.
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• W1521360157 date "1987-07-01" @default.
• W1521360157 modified "2023-10-01" @default.
• W1521360157 title "A monoclonal antibody to tissue plasminogen activator with affinity for the Kringle regions" @default.
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• W1521360157 doi "https://doi.org/10.1016/0268-9499(87)90001-4" @default.
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