Abstract
Cryogel produced duringcryofiltration consists mainly of a complex of fibrinogen (Fbg) and fibronectin (FN) (Cryofibrinogen: c-Fbg), which precipitates under cooling condition with heparin. EDA(+)FN (Cellular FN) is involved in the complex more specifically than plasma FN (pFN). To clarify the mechanisms of this specificity, we compared the binding rate (BR) of both fxbronectins onto immobilized Fbg as well as onto immobilized heparin at a temperature range of 4°C to 37°C. pFN showed a high BR onto both immobilized molecules at low temperatures. The BR of EDA(+)FN onto immobilized Fbg was modestly higher than that of pEN at each temperatures. The binding between EDA(+)FN and immobilized heparin showed a high BR even at high temperatures. In the cryoprecipitation study in vitro, EDA(+)FN showed a more rapid and higher cryoprecipitable character than that of pFN. In plasma removed of EDA(+)FN, Fbg didn't gel with heparin, but did with heparin upon the addition of EDA(+)FN. Therefore, EDA(+)FN appears to be essential in constructing c-Fbg during cryofiltration. Formation of the Fbg-FN-Heparin complex was caused more rapidly by the high cryoprecipitable potency of EDA(+)FN and the high affinity between EDA(+)FN and heparin at all temperature ranges in this study.
