Results 221 to 230 of about 76,398 (257)
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Activation of the classical complement pathway by BioRex-70

Immunology Letters, 1987
The cation exchange resin BioRex-70 was able to activate the classical complement pathway in human serum at 37 degrees C over the resin concentration range 0-5% (v/v). Using zymosan-treated human serum, it was found that the activation proceeded as far as complement protein C3.
R J, Vandenberg, S B, Easterbrook-Smith
openaire   +2 more sources

New insights into the molecular mechanisms of classical complement activation

Molecular Immunology, 2010
C1q, the initiator of the classical complement cascade, is a versatile molecule with numerous ligands and variety of functions. Recent mutagenesis, epitope mapping and structural data brought novel understanding of the molecular mechanisms of C1q binding to target molecules, and subsequent C1 activation.
Kenneth B M Reid
exaly   +3 more sources

An immunofluorescence assay for complement activation by the classical pathway

Journal of Immunological Methods, 1981
The functional integrity of classical complement pathway components was determined by an immunofluorescence (IFL) assay based on the capacity of cytoskeletal intermediate filaments (IMF) to bind C1q and to activate the complement pathway. The assay uses IMF-rich capillary endothelium of human term placentae as complement-activating substrate.
E, Linder, M, Rhen, S, Meri
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Paths reunited: Initiation of the classical and lectin pathways of complement activation [PDF]

open access: yesImmunobiology, 2010
Understanding the structural organisation and mode of action of the initiating complex of the classical pathway of complement activation (C1) has been a central goal in complement biology since its isolation almost 50 years ago. Nevertheless, knowledge is still incomplete, especially with regard to the interactions between its subcomponents C1q, C1r ...
Wilhelm Schwaeble   +2 more
exaly   +5 more sources

Activation of the classical pathway of complement by tobacco glycoprotein (TGP)

The Journal of Immunology, 1995
Abstract Tobacco glycoprotein (TGP), a polyphenol-rich glycoprotein isolated from tobacco leaves, activates the classical complement pathway through a mechanism that appears to involve direct interaction with C1q. A binding site on C1q for TGP can be localized by competitive inhibition with DNA to a region located in the junction ...
S M, Koethe, K E, Nelson, C G, Becker
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A microplate assay to measure classical and alternative complement activity

Clinical Chemistry and Laboratory Medicine (CCLM), 2017
AbstractBackground:We developed and validated a kinetic microplate hemolytic assay (HA) to quantify classical and alternative complement activity in a single dilution of human plasma or serum.Methods:The assay is based on monitoring hemolysis of sensitized sheep (or uncoated rabbit) red blood cells by means of a 96-well microplate reader.
Puissant-Lubrano, Bénédicte   +3 more
openaire   +3 more sources

Effects of anesthesia and operation on the classical pathway of complement activation

Clinical Immunology and Immunopathology, 1982
Abstract The present study examined whether anesthesia and operation could alter serum complement function as reflected by CH 50 levels and individual component activity. Classical complement pathway function was significantly reduced, as reflected by lowered CH 50 levels, in patients undergoing anesthesia and operation.
R E, Lewis, J M, Cruse, J V, Richey
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Succinylated and acetylated concanavalin A activate the classical complement pathway

Biochemical and Biophysical Research Communications, 1981
Abstract Succinylated and acetylated concanavalin A, but not the native lectin, lyse sheep erythrocytes in the presence of guinea pig complement. The effect appears to be specific since succinylated wheat germ agglutinin is inactive and hemolysis is inhibited selectively by α-D-methylglucopyranoside. Hemolytic activity is enhanced by preincubation of
J J, Langone, R, Ejzemberg
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Adiponectin binds C1q and activates the classical pathway of complement

Biochemical and Biophysical Research Communications, 2008
The adipose-specific protein adiponectin binds to a number of target molecules, including damaged endothelium and the surface of apoptotic cells. However, the significance of this binding remains unclear. This study demonstrates the binding of purified C1q to recombinant adiponectin under physiological conditions, and the dependence of this upon Ca(++)
Philip W, Peake   +3 more
openaire   +2 more sources

Activation of the Classic and Alternate Complement Pathways by Endotoxin

The Journal of Immunology, 1974
Abstract The ability of bacterial endotoxin (LPS) to activate the complement system was studied in guinea pig serum (GPS). In serum chelated with ethyleneglycol tetraacetic acid (EGTA) 10 mM, which permits alternate complement pathway activation but inhibits classic complement pathway activation, lysis of LPS-coated sheep erythrocytes (E-
openaire   +2 more sources

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