Results 161 to 170 of about 796,318 (197)

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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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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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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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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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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Genetic polymorphism of human C1R subcomponent of the first complement component in the Japanese population

Forensic Science International, 1988
Genetic polymorphism of the C1R subcomponent of human complement component C1 has been investigated in neuraminidase treated EDTA plasma samples of 440 healthy Japanese individuals living in Tokyo by means of thin-layer polyacrylamide gel isoelectric focusing (PAGIEF) at pH 3.5-9.5 in the presence of 8.0 M urea followed by an electroblotting with ...
Kazue Abe
exaly   +3 more sources

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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The binding and activation of the C1r-C1s subunit of the first component of human complement

Molecular Immunology, 1982
The value of the functional affinity constant between 125I-labelled Clq and the Clr-Cls tetramer (when free in solution) in the formation of Cl was found to be 3.6 × 107M−1. When Clq was bound to activating immune complexes, the value of K was about 10-fold higher before initiation of activation and there was a further two to three-fold rise as ...
N.C. Hughes-Jones, B.D. Gorick
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Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13

Human Genetics, 1988
C1r and C1s are distinct, but structurally and functionally similar, serine protease zymogens responsible for the enzymatic activity of the first component of complement (C1). Recent comparisons indicate a significant degree of sequence similarity between C1r and C1s and support the hypothesis that they are related by gene duplication.
V C, Nguyen, M, Tosi, M S, Gross, O, Cohen-Haguenauer, C, Jegou-Foubert, M F, de Tand, T, Meo, J, Frézal   +7 more
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Downregulation of C1R promotes hepatocellular carcinoma development by activating HIF‐1α‐regulated glycolysis

Molecular Carcinogenesis
C1R has been identified to have a distinct function in cutaneous squamous cell carcinoma that goes beyond its role in the complement system. However, it is currently unknown whether C1R is involved in the progression of hepatocellular carcinoma (HCC ...
Yuying Ma, Yuehua Wang, Peng Tuo, Zhongji Meng, Bin Jiang, Yahong Yuan, Yan Ding, Abid Naeem, Xingrong Guo, Xiaoli Wang   +9 more
semanticscholar   +1 more source