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- W2011292034 abstract "1.|The sequence of events occurring during proteolysis of fibrinogen by plasmin (EC 3.4.4.14) was followed by starch-gel electrophoresis, viscosity measurements and determination of nitrogen content in the thermolabile and thermostabile fibrinogen degradation products. The observed changes were related to the corresponding changes of anticlotting activity formed in the reaction mixture. 2.|In the early stage of proteolysis, maximal anticlotting activity was connected with the presence of a protein fragment, which seems to correspond to the recently described Fragment Y. In the late stage of proteolysis high molecular weight products are represented predominantly by Fragments D and E. These fragments seem to be linked together by non-covalent bonds, and are considered as the plasmin resistant core of the fibrinogen molecule. 3.|The formation of two moles of the core out of one mole of fibrinogen was concluded on the basis of the nitrogen balance of the degradation products, and molecular weight measurements. 4.|Sulphitolysis revealed that Fragment D is composed of several polypeptide chains whereas Fragment E contains only one polypeptide chain. 5.|A model of the fibrinogen macromolecule is proposed, according to which the sequence of the three polypeptide chains in the two subunits of the fibrinogen dimer is reversed." @default.
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- W2011292034 date "1967-10-01" @default.
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- W2011292034 title "High molecular weight products of the late stage of fibrinogen proteolysis by plasmin and their structural relation to the fibrinogen molecule" @default.
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- W2011292034 doi "https://doi.org/10.1016/0005-2795(67)90409-6" @default.
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