Plasmic degradation of human fibrinogen I. Structural characterization of degradation products

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Abstract

  • 1.

    1. Fragments X, Y, D, and E were prepared by plasmic degradation of human fibrinogen and purified by gel filtration and chromatography. Molecular weights of reduced polypeptide chains of fibrinogen and its degradation products were studied by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and urea.

  • 2.

    2. Plasmic hydrolysis of fibrinogen was interrupted at different digestion stages, and the release of polypeptides from fibrinogen was studied by polyacrylamide electrophoresis of non-reduced and reduced incubation mixtures.

  • 3.

    3. In the early phase of plasmic hydrolysis, the β and γ chains of fibrinogen lose small molecular weight peptides at the N-terminal and C-terminal ends, respectively. Large polypeptides are progressively being split from the C-terminal part of the α chain. Fragment X was found to be a heterogenous population of molecules differing in the length of their α chains.

  • 4.

    4. On further digestion, one pair of disulfide-bound β and γ chains is released from the fragment X, giving rise to Fragment Y, which in turn splits into another β-γ dimer and Fragment E. Our results suggest that the β-γ dimer corresponds to Fragment D and confirm the partial identity of Fragment E with the disulfide knot.

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