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C2 fragment + H2O
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C-terminal fragment originating from the processing of meningococcal proteases
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complement component C3 + H2O
complement component C3a + complement component C3b
complement component C3 zymogen + H2O
complement component C3b + complement component C3a
complement component C5 + H2O
complement component C5a + complement component C5b
complement component C5 zymogen + H2O
complement component C5b + complement component C5a
neisserial heparin binding antigen + H2O
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also known as GNA2132 (genome-derived Neisseria antigen 2132)
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t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester
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substrate of enzyme subunit Bb
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tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
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tert-butoxycarbonyl-norleucine-Gln-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-norleucine-Gln-Leu-Gly-Arg + 7-amino-4-methylcoumarin
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additional information
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 + H2O
complement component C3a + complement component C3b
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hydrolysis of peptide bond 77 Arg-Ser of the a-chain
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 is the preferred substrate. Cleavage of the preferred C3 substrate and deposition of C3b effectively switches the output of the enzyme from C3b to C5b, resulting in initiation of the cytosolic process of complement
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complement component C3 + H2O
complement component C3a + complement component C3b
analysis of structure and function of complement component C3b in complex with the macrophage-expressed complement receptor CRIg, CRIg shown as an inhibitor of alternative complement convertases
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complement component C3 + H2O
complement component C3a + complement component C3b
cleavage of complement component C3 mediated through the MBL pathway in human serum analyzed, mannan-binding lectin (MBL) promotes activation of C3, combined action of MBL-associated serine proteases MASP-1 and MASP-2 required, involvement of the alternative pathway not detected
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complement component C3 + H2O
complement component C3a + complement component C3b
interaction studies with decay-accelerating factor DAF mediating decay of the alternative pathway C3 convertase, C3bBb, but not of the inactive proenzyme C3bB
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complement component C3 + H2O
complement component C3a + complement component C3b
potencies of the amplification loop of the alternative complement pathway summarized
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complement component C3 + H2O
complement component C3a + complement component C3b
properdin-deficient patients susceptible to lethal meningococcal infection, studies on yet unknown mechanism of selective predisposition
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complement component C3 + H2O
complement component C3a + complement component C3b
studies on fluid-phase formation of initial convertase by fluorescence resonance energy transfer (FRET)
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 + H2O
complement component C3a + complement component C3b
cleavage of complement component C3 through the mannan-binding lectin pathway in mouse sera determined
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complement component C3 + H2O
complement component C3a + complement component C3b
complement activation in properdin-deficient mice analyzed
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complement component C3 + H2O
complement component C3a + complement component C3b
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complement component C3 zymogen + H2O
complement component C3b + complement component C3a
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complement component C3 zymogen + H2O
complement component C3b + complement component C3a
activation
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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methionine-modified enzyme has significantly lower C5-cleavage ability than that of unmodified enzyme
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 + H2O
complement component C5a + complement component C5b
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complement component C5 zymogen + H2O
complement component C5b + complement component C5a
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complement component C5 zymogen + H2O
complement component C5b + complement component C5a
activation
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additional information
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fragment Bb is the catalytic subunit of the enzyme, isolated Bb is unable to cleave either C3 or C5
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additional information
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the enzyme is involved in the alternative pathway of human complement
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additional information
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the activation peptide, C5a, possesses potent spasmogenic and chemotactic activity
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additional information
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the enzyme has a very short half-life. Dissociation of the two noncovalently bound subunits proceeds with a half-life of 1-3 min at 37°C under physiological conditions, and this rate increases greatly if regulatory proteins are present. Numerous decay-accelerating proteins are present in plasma and on host cells that bind to the noncatalytic subunit C3b and increase the rate at which the catalytic subunit Bb is released into the medium. Bb loses its enzymatic activity and its ability to bind to C3b upon release. Although C3b is able to rebind Bb and reform the enzyme, the interaction with most decay-accelerating factors also leads to permanent proteolytic interaction of the cell-bound subunit C3b by a fluid-phase protease Factor I. These regulatory events limit cleavage of C3, reduce release of the anaphylatoxin C3a and control the formation of more efficient C5 convertase enzymes
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additional information
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early complement stimulation in trauma patients analyzed, correlation with injury severity, tissue hypoperfusion and worse clinical outcomes identified
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additional information
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C3b binds uniformly to substances on the surface of Escherichia coli K12, whereas it shows a bimodal distribution on the surface of Staphylococcus aureus P209. Autoactivation activity of C3
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