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- W1991987206 abstract "The proteolysis of purified human fibrinogen by purified human plasmin was studied using polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Five major classes of high molecular weight breakdown products were resolved, with Products II-V resembling the previously described Fragments X, Y, D and E, respectively. Each class of products was heterogeneous. Six components of Product IV were resolved with conversion from higher to lower molecular weight as proteolysis proceeded. The sixth component was further degraded, especially in the presence of urea. The data were consistent with the following model. The mass of Product II (mol. wt 255 000) consisted of two molecules of Product IV (mol. wt 99 000) and one of Product V (mol. wt 56 000), while Product III (mol. wt 155 000) was composed of one molecule each of Product IV and V. The constituent polypeptide chains of Product IV were derived from C-terminal portions of β(B) and γ chains and an interior portion of the α(A) chain, one molecule of Product IV from each half-molecule of fibrinogen. Product V was constituted of fragments derived from N-terminal regions of all six chains of fibrinogen. The initially formed Product V contained both fibrinopeptide A moieties of fibrinogen but these were lost with further plasmin digestion." @default.
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- W1991987206 date "1972-05-01" @default.
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- W1991987206 title "A molecular model for the proteolysis of human fibrinogen by plasmin" @default.
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- W1991987206 doi "https://doi.org/10.1016/0005-2795(72)90043-8" @default.
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