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Characteristics of the Amyloid A Fibril‐Degrading Activity of Human Serum
Author(s) -
TEPPO A.M.,
MAURY C. P. J.,
WEGELIUS O.
Publication year - 1982
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.1365-3083.1982.tb00728.x
Subject(s) - diisopropyl fluorophosphate , chemistry , biochemistry , trypsin , elastase , enzyme , bovine serum albumin , serine protease , agarose , pancreatic elastase , microbiology and biotechnology , protease , biology
Radial diffusion in agarose gel containing amyloid A (AA) fibrils was used to study the scrum enzyme capable of degrading AA fibrils in vitro. This degradative activity was unaffected by soya bean trypsin inhibitor, tosyl‐lysine chloromethyl ketone, and gold thiomalale but was inhibited by bovine pancreatic trypsin inhibitor, phenylmethylsulphonylfluoride, diisopropyl fluorophosphate, α 1 ‐antitrypsin, and α 2 ‐macroglobulin, indicating that the enzyme involved is a serine protease. Agarose gel electrophoresis showed the enzyme to be an acidic protein with the same electrophoretic mobility as albumin, The molecular weight, measured by gel filtration, was approximately 50,000. The optimum pH of this enzyme was 7.3, and it was fairly heat‐resistant. The results suggest that the AA‐fibril‐degrading activity in human serum is due neither to elastase nor to cathepsin G. It has many characteristics in common with the enzymes unlike elastasu that are involved in the complete degradation of serum AA protein.