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We have analysed the polypeptide chain structure of soluble fibrin complexes in patients with pre-eclampsia and during defibrination with ancrod (Arvin). In pre-eclampsia soluble fibrin measured by fibrinogen-sepharose 4B chromatography was increased in comparison with normal pregnant women. The isolated fibrin contained intact α, β and δ chains but no crosslihked γ chains. A correlation (r = 0.959 P &lt;0.001) was found between the concentration of soluble fibrin and soluble complexes as measured by agarose gel filtration, suggesting these complexes consist mainly of fibrin-fibrinogen dimers. In vitro, the binding of soluble fibrin to fibrinogen-sepharose depended on the structure of the complexes and temperature. At 37°C intact fibrin, prepared with ancrod, was bound to the column, but fibrin lacking intact α chain could be eluted at 37°C. The soluble fibrin complexes in patients having therapy with ancrod could be separated into two;the greater part had reduced α chain and were eluted from the column at 3 7°C, whereas the smaller part had intact α chain and remained bound at 37°C. Bio-Gel A5m chromatography carried out at 37°C and 20°C also indicated that the major part of soluble complexes produced during ancrod defibrination were unstable at 37°C.

Analysis of Soluble Fibrin Complexes in Patients with Intra Vascular Coagulation