Abstract
The stabilization of fibrin clots by activated factor XIII involves two different sets of cross-linked chains. In one case (type I) two γ-chains are linked to each other, indicating that γ-chains have both donor (suitable lysyl-) and acceptor (suitable glutaminyl-) functions. A second system (type II) consists of a γ-chain linked to an α-chain. Experiments with a substitute donor (glycine ethylester) indicate that only γ-chains have enzyme-accessible acceptor sites, suggesting that α-chain participation is limited to lysyl side chains. A model molecular arrangement for fibrin has been suggested which accommodates all the data.
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Selected References
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