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- W143828102 abstract "This chapter describes the interaction between human granulocyte collagenase, elastase, and chymotrypsin-like cationic proteins and plasma protease inhibitors. In a study discussed in the chapter, granulocyte collagenase and elastase were inactivated by the formation of firm complexes with α 1 antitrypsin and also with α 2 -macroglobulin. The α 1 -antitrypsin complexes with the collagenase migrated like α 2 -glooulins on agarose gel electrophoresis and produced distinct, narrow precipitates on crossed immunoelectrophoresis with antiserum to α-antitrypsin. The corresponding α,-antitrypsin complexes with the more basic granulocyte elastase migrated as inter- β -globulins. The chymotrypsin-like cationic proteins are inhibited by complex formation with α 2 -macroglobulin and α 1 antitrypsin but also by α 1 -antichymotrypsin. This protein responds as an acute phase reactant on all types of acute destruction, α 1 -antichymotrypsin and C-reactive protein exhibit the most rapid acute phase responses and may exceed the upper limits of normal range within 8 hours. A molar combining ratio of 1:1 was observed for each inhibitor and enzyme besides α 2 macroglobulin." @default.
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- W143828102 date "1978-01-01" @default.
- W143828102 modified "2023-10-16" @default.
- W143828102 title "GRANULOCYTE PROTEASES, THEIR RELEASE AND INHIBITION IN THE BODY" @default.
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- W143828102 doi "https://doi.org/10.1016/b978-0-08-022628-6.50021-x" @default.
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