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Binding Characteristics of Human Serum Amyloid P Component
Author(s) -
SERBAN D.,
RORDORFADAM C.
Publication year - 1987
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1987.tb01073.x
Subject(s) - picric acid , chemistry , serum amyloid p component , bovine serum albumin , biochemistry , macromolecule , keyhole limpet hemocyanin , binding site , glycoprotein , plasma protein binding , biology , antibody , immunology , organic chemistry , c reactive protein , inflammation
Serum amyloid P comptinent (SAP), a normal human plasma glycoprotein. was found in a solid phase ELISA to have Ca 2+ ‐dependent binding for keyhole limpet haemocyanin (KLH), pectic acid, trinitrophenylated (TNP) maeromolecules, and plastic surfaces. The binding U) TNPKLH was used to develop a sensitive ELISA. The binding of SAP to the ligands mentioned was inhibited by EDTA, KLH, pectic acid, TNP‐conjugated macromolecules (bovine serum albumin, polyacrylhydrazide), and p‐nitrophenylarsonic acid, Underivatized and DNP‐conjugated macromolecules did not inhibit the SAP binding; arsenilic acid, picric acid, and dinitrophenyl were weak inhibitors. SAP bound to TNP‐agarose was eluated by either EDTA or p‐nitrophenylarsonic acid. Thus, a unique region of SAP is responsible for the polyspecific binding. We suggest that the polyspecific binding of SAP takes place through a Ca 2+ bridge: half of the metal coordination sphere is occupied by SAP. with the other half available to interact with metal ligand.