Modified C-reactive protein selectively binds to immunoglobulins.
作者： M. Boncler , D. Dudzińska , J. Nowak , C. Watała
DOI: 10.1111/J.1365-3083.2012.02704.X
关键词:
摘要: Modified C-reactive protein (mCRP) has been reported to non-specifically bind immunoglobulins; notwithstanding, the nature of these interactions is not clear. The aim this study was investigate binding antibodies directed against HSA and IgG mCRP, fibrinogen (Fg), IgG, fibronectin (Fn) C1q its contaminants. We also studied mCRP towards receptors involved in CRP signalling (anti-CD32, anti-CD16). For analysis such interactions, a combination ELISA Western immunoblotting applied. tested powerfully bound either contaminations purified proteins (Fg, Fn mCRP) or interacted directly with some (C1q, Fg). effectiveness anti-HSA immobilized influenced by antigenic specificity antibody, content various fractions contaminants given (albumin augmented interactions), overall purity natural avidity immunoglobulins. relative anti-IgG considerably lower than that observed for plasma proteins. Furthermore, strength direct interaction between immunoglobulins varied from lack response (anti-HSA) negligible (anti-IgG) relatively high signal (human anti-CD16, anti-CD32), as compared control. Based on observations, we conclude cannot be easily generalized kind universal phenomenon.
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