Human platelet fibrinogen: purification and hemostatic properties. Blood

Conditions were developed in which 80 % to 90 % of platelet fibrinogen could be routinely purified in nondegraded form from the fluid phase of platelet suspensions stimulated with the calcium ionophore. A231 87, in the presence of calcium. leupeptin, and prostaglandin E1. Fibrinogen was separated from other released proteins by chromatogra-phy on diethylaminoethanol (DEAE)-cellulose using a con-tinuous pH and ionic strength gradient. Purified platelet fibrinogen,>98 % homogeneous by immunoelectrophoresis and sodium-dodecyl sulfate-polyacrylamide gel electropho-resis (SDS-PAGE), consisted of intact Aa, Bfi and y chains, but not ‘y ’ chains, and was 95 % to 96 % clottable. A T LEAST two physically distinct pools of human fibnin-ogen exist: plasma fibninogen, synthesized by the liver and contained in the circulating blood plasma fnaction3; an