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Degradation of Amyloid Proteins by Different Serine Proteases
Author(s) -
SKOGEN B.,
NATVIG J. B.
Publication year - 1981
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.1365-3083.1981.tb00579.x
Subject(s) - chemistry , plasmin , kallikrein , sephadex , proteases , biochemistry , size exclusion chromatography , enzyme , serine protease , macroglobulin , chromatography , elastase , serine , molecular mass , immunodiffusion , fractionation , thrombin , protease , biology , genetics , platelet , antigen , immunology
A protein extract was obtained from normal human serum by adsorption to unsubstituted Sepharose 4B. This extract contained one or several enzymes with SAA and AA degrading capacity. The optimal pH for degradation of SAA was about 7.3. On fractionation of the enzyme extract on Sephadex G‐150, the active component Was eluted in the V 0 peak. The V 0 fraction, which on double immunodiffusion analysis was found to contain α 2 ‐macroglobulin, was also active against synthetic substrates used to determine the activity of thrombin and plasma kallikrein. Gel filtration under dissociating conditions and molecular weight estimation further indicated the presence of those enzymes in the preparation. Several serine proteases which are known to be inhibited by α 2 ‐macroglobulin possessed AA and SAA degrating activity. On degradation of SAA, an intermediate split product with molecular weight similar to AA was formed. Kallikrein, plasmin and elastase were also able to degrade intact amyloid fibrils suspended in phosphate‐buffered saline