The covalent-binding reaction of complement component C3
نویسندگان
چکیده
منابع مشابه
Compstatin, a peptide inhibitor of complement, exhibits species-specific binding to complement component C3.
Although activation of complement protein C3 is essential for the generation of normal inflammatory responses against pathogens, its unregulated activation during various pathological conditions leads to host cell damage. Previously we have identified a 13-residue cyclic peptide, Compstatin, that inhibits C3 activation. In this study, we have examined the species-specificity of Compstatin. Bimo...
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Patients with multiple myeloma (MM) are at an increased risk for infections with bacteria that require opsonization with complement. Because Streptococcus pneumoniae is the most frequently encountered pathogen in these patients, we investigated the ability of serum from patients with MM to mediate the binding of C3b, the major opsonin of the complement system, to S. pneumoniae. S. pneumoniae ty...
متن کاملEcoRI polymorphism in the human third complement component (C3) gene.
Source/Description A cDNA fragment, pC3.11 (1) was used as probe. Polymorphisms: EcoRI cleavage of genomic DNA reveals a 2 allele polymorphism with band sizes of 5.2 and 5.6 kb. Invariant bands of 11.5, 11.0, 9.0 and 3 0 kb were also present. Frequency: Estimated from 35 unrelated Caucasians. Allele Frequency Dl 5.2 0.67 D2 5.6 0.33 Chromosomal Localisation: The human C3 gene had been assigned ...
متن کاملPhylogeny of the third complement component, C3, and conservation of C3-ligand interactions.
Of the 30 distinct complement proteins recognized to date, C3 is probably the most versatile and multifunctional molecule known, interacting with at least 20 different proteins.'s2 It plays a critical role in both pathways of complement activation and participates in phagocytic and immunoregulatory processes.'V2 The study of C3 molecules from different species gives insight into the structural ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1981
ISSN: 0264-6021
DOI: 10.1042/bj1930115