Open AccessS protein binds to serum‐treated agarose beads independently of complement activation and the formation of the terminal complement complex on the beads
Author(s) -
HETLAND G.,
GARRED P.,
PETTERSEN H. B.,
MOLLNES T.E.,
JOHNSON E.
Publication year - 1990
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1990.tb08112.x
Subject(s) - agarose , radioimmunoassay , microbiology and biotechnology , classical complement pathway , complement system , blot , immunoassay , monoclonal antibody , antibody , chemistry , sepharose , protein g , enzyme , biology , biochemistry , immunology , gene
SUMMARY Comparison of initial fearly‐phased and terminal (late‐phase) sequence activation of complement by agarose beads and endotoxin was evaluated in an enzyme immunoassay (EIA) of serum levels of C3c and C9 neoepitopes. Respectively. EIA and Western boloting with anti‐S protein monoclonal antibody revealed lower S protein values and weaker S protein bands in serum activated by agarosebeads than by endotoxin implaying that S protein was removed from serum by binding to agarose. The binding of S protein to the beads was confirmed by radioimmunoassay and was found to be equal m normal and heat‐inactivated serum. In contrast, the terminal complement complex was formed only on agarose heads invubated with normal serum and not with inactivated serum.