Results 181 to 190 of about 27,085 (217)
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Complement C3b interactions studied with surface plasmon resonance technique
International Immunopharmacology, 2001The surface plasmon resonance (SPR) phenomenon is utilized in a number of new real time biosensors. In this study, we have used this technique to study interactions between the central complement component C3b and its multiple ligands by using the Biacore equipment.
T S Jokiranta +2 more
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Inhibition of complement by covalent attachment of rosmarinic acid to activated C3b
Biochemical Pharmacology, 1999Rosmarinic acid has been reported to inhibit complement activation in vivo as well as in vitro. Previous studies suggested that the inhibitory effect was due to inhibition of C3/C5 convertases, but inhibition of C3b attachment would yield the same results.
A, Sahu, N, Rawal, M K, Pangburn
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An investigation of the interaction between human complement factor H and C3b
Biochemical Society Transactions, 1995The complement system in human blood is a major effector system in humoraVinnate immunity (1). Factor H is a 155kD glycoprotein which is involved in the regulation of the complement alternative pathway (2). Factor H regulates C3 turnover by 2 activities: decay acceleration activity describes the ability of factor H to bind to C3b thus displacing Bb ...
C J, Soames, R B, Sim
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C3b and factor H: key components of the complement system
Expert Review of Clinical Immunology, 2006In all three complement pathways, the central molecule is C3, which, upon activation cleavage, forms the major opsonin C3b - the key component of complement. C3b is also essential for propagation of the complement cascade to the stage of the lytic terminal complement complexes.
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Methods for assaying nine bovine complement components and C3b-inactivator
Molecular Immunology, 1980Abstract Methods are presented for titrating bovine C3b-inactivator, C2, C3 and C4† by non-hemolytie means, and for assaying all the components of bovine complement except C2 by hemolysis. All components were detected at serum dilutions above 1:1000, and some at dilutions above 1:100,000.
W D, Linscott, R P, Triglia
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Interaction of C3b, B, and D̄ in the Alternative Pathway of Complement Activation,
The Journal of Immunology, 1975Abstract The interaction of ZXd2, an insoluble intermediate of the alternative pathway on zymosan (Z5), with factor B and the enzyme D̄ proceeds in a two-step reaction: 1) B binds in the presence of Mg++ to ZXd2 to form the intermediate ZXd2B, 2) B bound to ZXd2 is subsequently activated enzymatically by D̄ to yield the complex ZXd2B ...
A, Nicholson +5 more
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Associated complement C3b. Towards an understanding of its intracellular modifications
Molecular Immunology, 1993Covalent Superose microspheres-bound C3b was used as a model system to simplify the analysis of antigen-bound C3b modifications during antigen processing. The model was set up using purified C3 and Superose-bound trypsin. C3b was covalently bound to Superose through an ester link, as indicated by lability to hydroxylamine treatment at alkaline pH.
C A, Rey-Millet, S, Chesne, M G, Colomb
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The Journal of Immunology, 1979
Abstract Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and β1H globulin (β1H) cleaved the α-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact β-chain (C3bi). Subsequent treatment with trypsin (0.1 µg/ml) released 125I into the supernatant and yielded cells
Jaime R Carlo +3 more
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Abstract Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and β1H globulin (β1H) cleaved the α-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact β-chain (C3bi). Subsequent treatment with trypsin (0.1 µg/ml) released 125I into the supernatant and yielded cells
Jaime R Carlo +3 more
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The Journal of Immunology, 1989
Abstract Tumor cells have adapted several strategies which permit them to grow in an immunologically hostile environment. The C system can potentially destroy these cells; however, its action needs to be specifically potentiated on the surface of the tumor cells. To this end, a heteroconjugate composed of a mouse mAb and of the human C3b
Y, Reiter, Z, Fishelson
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Abstract Tumor cells have adapted several strategies which permit them to grow in an immunologically hostile environment. The C system can potentially destroy these cells; however, its action needs to be specifically potentiated on the surface of the tumor cells. To this end, a heteroconjugate composed of a mouse mAb and of the human C3b
Y, Reiter, Z, Fishelson
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Computational Study of the Binding Mechanism of Complement C3b with Antigen
Bulletin of the Chemical Society of Japan, 2013Abstract The reaction mechanism of the covalent binding of complement component 3 (C3) with antigen, which significantly contributes to the immune system by enhancing the phagocytosis of phagocytes, is examined by density functional theory (B3LYP).
Toshiaki Matsubara, Chisato Sasamoto
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