COAGULATION AND HEMOSTATIC EFFECTS OF DEXTRAN AND OTHER MACROMOLECULES.
Abstract
An attempt was made to explain the long-known hemostatic defect associated with the infusion of dextran (D) and other blood substitutes. No clotting abnormalities are demonstrable by orthodox techniques that singly, or additively, explain the abnormality. Paradoxically, D, hydroxyethyl starch (HES), gelatin, modified fluid gelatin (Plasmagel), polyvinyl pyrollidone, polyserine, polyglutamic acid, morpholinylethyl glutamimide (PAMEG) accelerate plasma or fibrinogen (F I) clotting by thrombin. In contrast, albumin, Hgb, modified fluid gelatin crosslinked polypeptide (Haemaccel), and oxypolygelatin (Gelifundol), are relatively inert. D, HES, and some of the other macromolecules precipitate a substantial amount (but not all) of plasma F I and F VIII, or purified F I. The precipitate is indistinguishable from the F VIII-rich cryoprecipitate obtained in slow-thawing frozen plasma used for hemophilia therapy. The D- or HES-precipitated material behaves thereafter as a true cryofibrinogen, and thrombin clots it faster than the parent material. Although no clear-cut F I-D 'complex' can be demonstrated, it appears that the macromolecule by interaction has subtly altered the F I causing these abnormalities, or that the polymer precipitates a different species of F I (cryofibrinogen) in normal plasma. The latter possibility is in harmony with the observation that D-precipitable F I can be increasingly produced from purified F I that is timewise progressively exposed to miniscule amounts of thrombin. Naked latex particles are agglutinated by extremely minute amounts of soluble fibrin monomer in an F I-thrombin mixture. This aggregation is enhanced approx. 40x by D. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 25, 1969
- Accession Number
- AD0693883
Entities
People
- Benjamin Alexander
Organizations
- New York Blood Center