Measurement of the ‘fast’ or complexed form of α2 macroglobulin in biological fluids using a sandwich enzyme immunoassay
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2019, International Journal for ParasitologyCitation Excerpt :As a result of interaction with an endoprotease, the receptor recognition site for the low-density lipoprotein receptor-related protein (LRP) of A2M* becomes exposed (Strickland et al., 1990; Herz and Strickland, 2001). In vivo, the A2M*/protease complex is rapidly cleared by LRP-mediated endocytosis and subsequently degraded (Imber and Pizzo, 1981), so it typically represents less than 1% of the total A2M in blood plasma of adults (Banks et al., 1990). The trapped protease molecules become covalently linked to the A2M as a result of cleavage of a thioester bond in the cavity, but their enzymatic activity is retained at least with respect to small-sized molecules such as chromogenic substrates that can pass through the arms of the proteinase-trapping cage (Barrett and Starkey, 1973; see also Fig. 1C).
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2017, Clinical BiochemistryCitation Excerpt :By native PAGE, we demonstrated that the antibody 16-11-17 specifically recognized F-α2M but not N-α2M. Furthermore, we showed that 16-11-17 recognizes rRBD of human α2M which is only exposed in F-α2M [12–14]. Using this antibody, an ELISA measuring F-α2M was established.
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2016, Fish and Shellfish Immunology