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- W1996918082 abstract "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 activation proceeded. The addition of an excess of unlabelled Clq increased the rate of activation of 125I-labelled Cl, suggesting an interaction between Clr-Cls and two neighbouring Clq molecules. It is suggested that the tetramer Clr-Cls may bind bivalently to Clq when free in solution, but on binding to activating complexes, one of the Clr-Cls binding sites is detached from Clq and becomes bound to a site on the complex. The resultant spatial rearrangement of the Clr molecules within the tetramer may be optimal for autocatalytic activation of Clr." @default.
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- W1996918082 date "1982-09-01" @default.
- W1996918082 modified "2023-09-27" @default.
- W1996918082 title "The binding and activation of the C1r-C1s subunit of the first component of human complement" @default.
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- W1996918082 doi "https://doi.org/10.1016/0161-5890(82)90321-2" @default.
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