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Kinetics of interaction of C1 inhibitor with complement C1s.
Biochemistry, 1986The 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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C1 inhibitor: different mechanisms of reaction with complement component C1 and C1s.
Immunological investigations, 1991Inactivation 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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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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