Results 221 to 230 of about 277,579 (267)
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Identification of the disulfide bonds of human complement C1s
Biochemistry, 1991C1s, one of the three subcomponents of C1, the first component of the complement system, is a complex serine protease. To determine the disulfide-bonding pattern, fragments of C1s were generated by cleavage with pepsin, thermolysin, or subtilisin.
Hess D, Schaller J, Rickli EE
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Detection of complement C1-inhibitor with a piezoelectric immunosensor
Fresenius' Journal of Analytical Chemistry, 2001A novel piezoelectric immunosensor has been developed for the detection of human complement C1-inhibitor. Anti-C1-inhibitor antibody was immobilized onto the gold electrodes of a 9 MHz AT-cut piezoelectric crystal. Coating the crystal with polyethyleneimine adhesion, followed by a glutaraldehyde cross-linking method to immobilize antibody showed better
L, Liu, J, Hu, L, Wang, L, Liu, X, Zhou
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The Journal of Immunology, 1977
Abstract An equilibrium between free C1s and C1s bound in macromolecular C1 exists in human serum. This equilibrium can be utilized to incorporate radioiodinated C1s into serum C1. Human sera were incubated for 40 hr at 4°C with 125I-C1s to allow the exchange between free and bound C1s to reach equilibrium. The C1 complex labeled in this
R M, Bartholomew, A F, Esser
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Abstract An equilibrium between free C1s and C1s bound in macromolecular C1 exists in human serum. This equilibrium can be utilized to incorporate radioiodinated C1s into serum C1. Human sera were incubated for 40 hr at 4°C with 125I-C1s to allow the exchange between free and bound C1s to reach equilibrium. The C1 complex labeled in this
R M, Bartholomew, A F, Esser
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Subunit interactions in the first component of complement, C1
Biochemical and Biophysical Research Communications, 1987Interactions between C1q and other subunits of C1 were analyzed by sucrose gradient ultracentrifugation. A zone of dilute, radioiodine labelled C1q was sedimented through uniform concentrations of either C1r2C1s2, C1r2, C1r2 or C1s(2). The dissociation constants were found to be 3 x 10(-9) M and 6 x 10(-9) M for C1r2C1s2 and C1r2 binding respectively ...
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Structure and activation of the C1 complex of complement: unraveling the puzzle
Trends in Immunology, 2004Abstract C1, the multimolecular protease that triggers the classical pathway of complement, has a major role in the host defense against pathogens. It also participates in other biological functions, such as immune tolerance, owing to the ability of its binding subunit, C1q, to recognize abnormal structures from self, including apoptotic cells ...
Christine, Gaboriaud +5 more
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The first component of human complement (C1): Activation and control
Springer Seminars in Immunopathology, 1983The first component of human complement (C1) is a 750 000 dalton glycoprotein that requires calcium or other specific metal ions to maintain its native structure and function. Under physiologic conditions, C1 comprises two weakly interacting subunits, C1q and C1r2s2, with C1q containing the binding site(s) for activators and C1r2s2 possessing enzymatic
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Assembly and Activation of the C1 Complex of Complement
2022Complement is an essential component of the innate immune system. The classical pathway of complement activation is initiated by the 774 kDa C1 complex. The C1 complex comprises two C1r and two C1s serine proteases, synthesised as zymogens and arranged as a C1s-C1r-C1r-C1s, Ca2+ dependent, heterotetramer bound to the centre of one C1q molecule.
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Arrangement of the C1 complex of complement
Biochemical Society Transactions, 1990G J, Arlaud, N M, Thielens, C, Illy
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