Abstract
High molecular weight end-products of fibrinogen proteolysis by plasmin (EC 3.4.3.14) were found to contain almost all of the disulphide bridges present in the parent molecule. Treatment of Fragments D and E from bovine fibrinogen with CNBr decreases their mol. wt from 80 300 to 34 000 and from 47 900 to 33 000, respectively. It does not, however, change the amount of half-cystines in the product derived from E, and splits off only 4 out of 12 of the original half-cystines present in Fragment D. A mutual relationship between the N-terminal disulphide knot of fibrinogen and Fragments D and E as well as their possible localization in the fibrinogen molecule are discussed.
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