Human cathepsin G. Catalytic and immunological properties
نویسندگان
چکیده
منابع مشابه
Britain Human Lysosomal Elastase CATALYTIC AND IMMUNOLOGICAL PROPERTIES
1. The elastase of human spleen was shown to exhibit endopeptidase activity against azocasein and elastin. 2. Activity against several synthetic substrates was detected, and benzyloxycarbonyl-L-alanine 2-naphthyl ester was found to be a good substrate for routine use. 3. The enzyme showed a broad pH optimum in the range of 8.2-9.2 against azo-casein and the synthetic substrate. 4. The effect of...
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Leukocyte cathepsin G (CLP) and elastase (ELP) from human blood were partially purified, and enzymatic properties of CLP and a2-macroglobulin-CLP complex (a2M-CLP) were studied in comparison with those of ELP and a2M-ELP. Furthermore, some synthetic substrates and synthetic reversible inhibitors for CLP were newly synthesized and specificities for CLP were compared with those of a-chymotrysin. ...
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Cathepsin G (CatG), a serine protease found in the azurophil granules of neutrophils, participates in killing engulfed microorganisms. CatG is a poorly understood enzyme, in part because it can only be obtained as mature enzyme purified from human blood, and because it seems to have dual specificity for chymotrypsin-like and trypsin-like substrates. Therefore, yeast Pichia pastoris was used to ...
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Cathepsin L variants purified from sheep and ox liver are shown to have similar catalytic properties to those from rat, rabbit and man with regard to activity against the substrate benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide and inhibition by benzyloxycarbonyl-Phe-Phe-diazomethane, thus identifying cathepsin L in these species for the first time. All five variants of cathepsin L are sho...
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Polymorphonuclear leukocytes (PMN) when activated release products that can potentially injure endothelial cells or alter endothelial function. Exposure of cultured human umbilical vein endothelial cells to cathepsin G and elastase isolated from human PMN at concentrations reached in vivo (100 ng/mL to 10 micrograms/mL) selectively inhibited thrombin-induced prostacyclin production and the thro...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1976
ISSN: 0264-6021
DOI: 10.1042/bj1550273