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- W4229508067 abstract "This chapter focuses on the structure and function of fibrinogen, a soluble plasma protein cleaved by thrombin to produce an insoluble fibrin clot. Polymerization to form fibrin also acts as a cofactor in platelet aggregation. The chapter presents details of this molecule, which is a hexamer that contains two sets of nonidentical chains (α, β, and γ) linked to each other in an antiparallel arrangement by disulfide bonds. The α chain protuberance and the coiled-coils together account for half of the mass of a fibrinogen molecule. Fibrinogen can be purified by a modified cold ethanol fractionation and the individual chains separated by carboxymethylation in 6M guanidine-HCl and CM-cellulose chromatography in 8M urea. The chapter discusses the gene structure of the α chain of fibrinogen." @default.
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- W4229508067 date "1998-01-01" @default.
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- W4229508067 title "Fibrinogen" @default.
- W4229508067 doi "https://doi.org/10.1016/b978-012068911-8/50131-7" @default.
- W4229508067 hasPublicationYear "1998" @default.
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