Results 161 to 170 of about 375,488 (189)

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
openaire   +2 more sources

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 ...
Katsunori Akiyama
exaly   +3 more sources

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
openaire   +2 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
openaire   +2 more sources

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
openaire   +1 more source

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
openaire   +2 more sources

Non-coordinated biosynthesis of early complement components in a deficiency of complement proteins C1r and C1s.

Scandinavian journal of immunology, 1994
We report on a 60-year-old woman with systemic lupus erythematosus and a total (95%) C1r and a partial (36%) C1s deficiency. The patient complained about cutaneous lesions on forearms and legs without other systemic involvement. Elevated anti-nuclear, anti-native DNA and anti-SSA antibodies were present.
A, Chevailler, C, Drouet, D, Ponard, C, Alibeu, S, Suraniti, F, Carrère, G, Renier, D, Hurez, M G, Colomb   +8 more
openaire   +1 more source

A polymorphism detected in sheep using a complement subcomponent C1r (C1R) probe

Journal of Animal Science, 1995
S H, Phua, N J, Wood
openaire   +2 more sources

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
openaire   +1 more source

A common amino acid polymorphism in complement component C1R

Human Molecular Genetics, 1994
M M, Nöthen, G, Dewald
openaire   +2 more sources