Results 131 to 140 of about 5,097 (156)

An Improved Method for Complement Subcomponent C1R Typing

Journal of Forensic Sciences, 1990
Abstract An improved method has been developed for the reliable classification of different C1R genetic variant forms from human serum or plasma. The method combines the use of neuraminidase-digested samples followed by monodimensional isoelectric focusing in the pH range 5 to 8 followed by immunoblotting.
M I, Kamboh, R E, Ferrell
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Characterization of the activation of the human C1r complement molecule

Molecular Immunology, 1982
The proenzyme form of C1r was isolated by sequential chromatography from the euglobulin fraction of human serum on DEAE-Sepharose 6B-CL, CM-Sepharose 6B-CL and Sepharose S-300-CL. This C1r had the tendency to spontaneously activate within 60-90 min of incubation at 37 degrees C in presence of EDTA and more slowly in the presence of Ca2+.
J, Bauer, G, Valet
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Nucleotide sequence of the cDNA coding for human complement C1r

Biochemistry, 1986
C1r is a zymogen of a serine protease that is involved in the activation of the first component of the classical pathway of the complement system. cDNAs coding for human C1r have been isolated from libraries prepared from poly(A) RNA from human liver and Hep G2 cells.
S P, Leytus, K, Kurachi, K S, Sakariassen, E W, Davie   +3 more
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Isolation of human complement subcomponents C1r and C1s in their unactivated, proenzyme forms

Journal of Immunological Methods, 1991
We have modified a standard isolation procedure for C1r and C1s, which employs IgG-Sepharose affinity chromatography followed by DEAE chromatography. As usual, all steps were performed at low temperature and two proteolytic inhibitors, PMSF and NPGB, were added during affinity chromatography on IgG-Sepharose.
P D, Lane, V N, Schumaker, Y, Tseng, P H, Poon   +3 more
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Physicochemical and Functional Characterization of the C1r Subunit of the First Complement Component

The Journal of Immunology, 1976
Abstract C1r was isolated from serum by an improved method and found to be a glycoprotein with a sedimentation coefficient of 7.0S. Under conditions of physiologic ionic strength and pH, C1r consists of two apparently identical noncovalently linked 95,000 dalton polypeptide chains.
R J, Ziccardi, N R, Cooper
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A polymorphism in the complement component C1r is not associated with sporadic Alzheimer's disease

Neuroscience Letters, 2003
A growing body of evidence suggests that Alzheimer's disease (AD) is associated with local inflammation processes. Complement activation is one of the cardinal pathological features of the inflammation. Intensive AD association studies investigating polymorphisms in inflammatory-related genes have been recently performed, mainly in cytokines, but much ...
Hanna, Rosenmann, Zeev, Meiner, Esther, Kahana, Zoja, Aladjem, Gideon, Friedman, Arie, Ben-Yehuda, Tal, Grenader, Eli, Wertman, Oded, Abramsky   +8 more
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Ca(2+)-linked association of human complement C1s and C1r.

Biochemistry, 1994
The weight-average molecular weight of Clr, an activated serine protease subcomponent of complement Cl, was measured in the presence of widely varying concentrations of Ca2+ and the other serine protease subcomponent, Cls, by utilizing the technique of tracer sedimentation equilibrium.
G, Rivas, K C, Ingham, A P, Minton
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Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions

Molecular Immunology, 2009
C1r, C1s and the mannose-binding lectin-associated serine proteases (MASPs) are responsible for the initiation of the classical- and lectin pathway activation of the complement system. These enzymes do not act alone, but form supramolecular complexes with pattern recognition molecules such as C1q, MBL, and ficolins.
Péter, Gál, József, Dobó, Péter, Závodszky, Robert B M, Sim   +3 more
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Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r

Molecular Immunology, 2008
C1r is a modular serine protease which is the autoactivating component of the C1 complex of the classical pathway of the complement system. We have determined the first crystal structure of the entire active catalytic region of human C1r. This fragment contains the C-terminal serine protease (SP) domain and the preceding two complement control protein (
József, Kardos, Veronika, Harmat, Anna, Palló, Orsolya, Barabás, Katalin, Szilágyi, László, Gráf, Gábor, Náray-Szabó, Yuji, Goto, Péter, Závodszky, Péter, Gál   +9 more
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One Active C1r Subunit Is Sufficient for the Activity of the Complement C1 Complex: Stabilization of C1r in the Zymogen Form by Point Mutations

The Journal of Immunology, 1999
Abstract The binding of C1 (the first component of complement) to immune complexes leads to the autoactivation of C1r through the cleavage of the Arg463-Ile464 bond in the catalytic domain. Spontaneous activation of C1r (and C1) also occurs in the fluid phase, preventing the characterization of the zymogen form of C1r.
J, Dobó, P, Gál, K, Szilágyi, S, Cseh, Z, Lörincz, V N, Schumaker, P, Závodszky   +6 more
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