Abstract
Abstract The digestion of fibrinogen by trypsin, as followed in the pH-stat, can be described in terms of three distinct reaction classes: (a) A fast reaction involving the splitting of 12 peptide bonds during which clottability is lost, (b) a slower reaction involving 80 peptide bonds, associated with the appearance of a slower sedimenting component in the ultracentrifuge and indicating the production of large fragments, and (c) a slow reaction which covers the remaining bonds susceptible to trypsin and which results in the fragmentation of the molecule into small peptides. The digestion was also followed in the viscosimeter, ultracentrifuge and polarimeter, and the liberation of non-protein nitrogen measured. The disappearance of clotting ability associated with the first phases of the reaction was studied, and certain conclusions were drawn concerning the mechanism of this inactivation process.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects
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