Results 101 to 110 of about 5,894 (144)

Kinetics of interaction of C1 inhibitor with complement C1s.

Biochemistry, 1986
The kinetics of inhibition of the complement serine protease, C1s, by its only known inhibitor, C1 inhibitor, have been measured by a variety of methods. One method continuously monitors the loss of esterolytic activity with a synthetic substrate coupled to a chromogen while another monitors the formation of a stable (covalent) complex by high-pressure
M, Lennick, S A, Brew, K C, Ingham
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Molecular Basis of Human Complement C1s Deficiency

The Journal of Immunology, 1999
Abstract This is the first report on the molecular basis of human complement C1s deficiency. Two abnormalities in the C1s gene were identified in a Japanese family, including one patient, by using exon-specific PCR, single-strand conformation polymorphism analysis, and nucleotide sequencing. A deletion of 4 bp, TTTG, was identified in
Y, Endo, K, Kanno, M, Takahashi, K i, Yamaguchi, Y, Kohno, T, Fujita   +5 more
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Functional model of subcomponent C1 of human complement

Journal of Molecular Biology, 1986
The domain organization of the zymogen subunits of the first component of human complement C1s, C1r2 and the complex C1s-C1r2-C1s was studied by electron microscopy. In the absence of Ca2+, monomeric C1s was visualized as a dumb-bell-shaped molecule consisting of two globular domains (center-to-center distance 11 nm) connected by a rod.
V, Weiss, C, Fauser, J, Engel
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Clionasterol: A Potent Inhibitor of Complement Component C1

Planta Medica, 2003
Clionasterol (1a), clionasterol monoacetate (1b) and 5alpha,8alpha-epidioxy-24alpha-ethylcholest-6-en-3-ol (2), isolated from the marine sponge Xestospongia exigua, and beta-sitosterol (3) were tested for their influence on the classical (CP) and alternative (AP) pathways of activation of the human complement system in vitro.
Fátima, Cerqueira, Rawiwan, Watanadilok, Pichai, Sonchaeng, Anake, Kijjoa, Madalena, Pinto, Henriette, Quarles van Ufford, Burt, Kroes, Cees, Beukelman, Maria São José, Nascimento   +8 more
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Identification of the disulfide bonds of human complement C1s

Biochemistry, 1991
C1s, 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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C1 inhibitor: different mechanisms of reaction with complement component C1 and C1s.

Immunological investigations, 1991
Inactivation of human complement subcomponent C1-s by its regulator C1 inhibitor at physiological ionic strength proceeded at a 3-fold higher rate when C1-s was in the physiological C1- complex with subcomponents C1q and C1-r rather than as purified subunit.
G L, Hortin, B L, Trimpe
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Detection of complement C1-inhibitor with a piezoelectric immunosensor

Fresenius' Journal of Analytical Chemistry, 2001
A 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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Subunit interactions in the first component of complement, C1

Biochemical and Biophysical Research Communications, 1987
Interactions 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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Arrangement of the C1 complex of complement

Biochemical Society Transactions, 1990
G J, Arlaud, N M, Thielens, C, Illy
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The first component of human complement (C1): Activation and control

Springer Seminars in Immunopathology, 1983
The 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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