Abstract
Fibrin clots obtained from diluted human plasma with bovine thrombin often contain amounts of phospholipids that cannot be diminished by further plasma dilution. The [image]cold insoluble residue[image] obtained during fibrinogen preparation has a higher phosphorus content than the purified fibrinogen. Evidence showed that adsorption of phospholipids or phosphorus-containing fibrinopeptides on purified fibrinogen or fibrin was unlikely. O-Phosphorylserine was detected in acid hydrolysates of human fibrin. On the basis of phosphorus determinations the average molecular weight of human fibrinogen cannot be less than 342000 (304000-383000) for a group of ten donors, and 265000 for two other persons, assuming 1 phosphorus atom/molecule and incomplete splitting of the phosphorus-containing fibrinopeptide. Complete splitting of the phospho-peptide would require molecular weights twice as high. Fibrinolysis was a possible cause of lower phosphorus contents found in isolated fibrinogen and fibrin from a donor who showed apprehension during blood collection and in a fibrinogen preparation that had been submitted to prolonged dialysis.

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