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Fibrinogen and the cold-insoluble globulin of plasma (CIg) are the main protein components of the heparin cryoprecipi table fraction (HPF) of normal plasma. The interactions between these proteins and heparin were examined. Heparin formed a cold precipitable complex with purified CIg or with mixtures of CIg and fibrinogen (T/2, 0.2; pH 7.2) but not with fibrinogen alone. Cryoprecipitation could be augmented by addition of Ca++ or by selection of optimal heparin levels; it could be reduced or even abolished by raising the ionic strength or pH or both, or by raising the heparin level above that needed for maximum precipitation of CIg. Fibrinogen reduced the threshold level of CIg at which heparin-induced cryoprecipitation occurred and, by co-precipitating with heparin and CIg, increased the total precipitate that formed. In contrast to the HPF from normal plasma which contained both fibrinogen and CIg, that from afibrinogenemic plasma contained CIg but lacked fibrinogen. Normal plasma depleted of CIg failed to form a heparin-induced cryoprecipitate. Thus, CIg is essential for heparin-induced cryoprecipitation to occur. Fibrinogen, as assessed by chromatographic experiments with heparin-Sepharose columns, has a considerably lower heparin-binding affinity than does CIg, indicating that it participates in formation of the HPF mainly, if not entirely, by virtue of its affinity for CIg.

Interactions Among Heparin, Cold-Insoluble Globulin, and Fibrinogen in Formation of the Heparin Precipitable Fraction of Plasma