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• W2032373343 endingPage "1226" @default.
• W2032373343 startingPage "1221" @default.
• W2032373343 abstract "The fixation of the third component of complement (C3) results in many important biological phenomenon, among which are (a) immune adherence (1), (b) enhancement of phagocytosis (2,3), (c) the release of an anaphylatoxin which is a potent releaser of histamine (4), and (d) the feedback activation of the alternative pathway (5,6). The physiological mechanisms involving C3 fixation require the generation of a C3 convertase which may occur by two separate pathways. C3 convertase can be generated, in the form of C42, by the so-called classical pathway of activation or in the form C3b,B by the alternative or properdin pathway (7). In both cases, C3 is converted to C3b by cleavage of a small peptide, C3a. Normal human serum contains an inactivator of activated C3b. This C2b inactivator or conglutinogen-activating factor (KAF) has been shown to inhibit both immune hemolysis and the immune adherence properties of C3b and to cause cleavage of C3b in the fixed and fluid- phase stages (8-11). Although it is known that the C3b inactivator is not depleted during its reaction with C3b and that C3b treated with the C3b inactivator becomes extremely sensitive to proteolytic digestion by trypsin and trypsin-like enzymes (9), the exact molecular nature of the action of the C3b inactivator on C3b has not been studied. In an effort to delineate the products of this interaction, purified C3b and C3b inactivator were allowed to react for various specific lengths of time and the products of these reactions were then analyzed." @default.
• W2032373343 created "2016-06-24" @default.
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• W2032373343 date "1975-05-01" @default.
• W2032373343 modified "2023-09-26" @default.
• W2032373343 title "The mechanism of action of the C3b inactivator (conglutinogen- activating factor) on its naturally occurring substrate, the major fragment of the third component of complement (C3b)" @default.
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• W2032373343 doi "https://doi.org/10.1084/jem.141.5.1221" @default.
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