Abstract
SAA is a major acute-phase protein comprising of 104 amino acids ciruclating in the plasma, assembled to subfraction of high density lipoproteins (HDL3). Two amyloid A proteins, NORl and NOR2, corresponding to residues 2–82 and 2–45, respectively, were extracted from an amyloidotic goiter of an FMF patient’s NOR. Three MoAbs against NOR2 were raised in mice. Two MoAbs recognize AA and SAA in addition to NOR2 and the third one recognizes NOR2 only. The binding of these MoAbs to NOR2 was inhibited by SAA-related peptides 2–82, 2–45, 2–15, 1–6. Almost no inhibition was observed with peptide 29–41. Two MoAbs recognize purified SAA dissolved in normal human sera. These MoAbs could not detect SAA in various acute-phase sera. Nevertheless, subjecting acute-phase HDL to denaturing conditions (SDS, urea) enables recognition of six SAA isoforms by these MoAbs. Supposing that denatured SAA is detached from HDL, these findings support the theory that the N-terminus of SAA functions as an anchor to the lipid layer of HDL.
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© 1991 Springer Science+Business Media Dordrecht
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Ziq-Bachar, Y., Levartowsky, D., Mordechaipras, Strachan, A.F., Fridkin, M., Smorodinsky, N.I. (1991). The N-Terminus is the Lipid-Binding Site of SAA: Supporting Evidence by MoAbs. In: Natvig, J.B., et al. Amyloid and Amyloidosis 1990. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3284-8_21
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DOI: https://doi.org/10.1007/978-94-011-3284-8_21
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