Some Effects of Low Molecular Weight Dextran on Coagulation

1966 ◽  
Vol 15 (01/02) ◽  
pp. 118-130 ◽  
Author(s):  
Marion Dugdale ◽  
J.D Nofzinger ◽  
F Murphey

SummaryLMDX has been shown to affect adversely the rate of prothrombin consumption during coagulation and the structure of the fibrin clot when present in the concentrations usually recommended for clinical use. Its use in animals with hemostatic defects induced by the pump-oxygenator was accompanied by excessive bleeding. At the same time, however, it conferred some form of protection which led to improved survival. A manner of using LMDX so as to benefit from its protective action without endangering hemostasis is currently under study.

2011 ◽  
Vol 5 ◽  
pp. PMC.S6803 ◽  
Author(s):  
Joel S. Goldberg

Low molecular weight opioid peptide esters (OPE) could become a class of analgesics with different side effect profiles than current opiates. OPE may have sufficient plasma stability to cross the blood brain barrier (BBB), undergo ester hydrolysis and produce analgesia. OPE of dipeptides, tyr-pro and tyr-gly conjugated to ethanol have a structure similar to the anesthestic agent, etomidate. Based upon the analgesic activity of dipeptide opioids, Lipinski's criteria, and permeability of select GABA esters to cross the BBB, opioid peptides (OP) conjugated to ethanol, cholesterol or 3-glucose are lead recommendations. Preliminary animal data suggests that tyr-pro-ethyl ester crosses the BBB and unexpectedly produces hyperalgesia. Currently, there are no approved OP analgesics available for clinical use. Clinical trials of good manufacturing practice OP administered to patients suffering from chronic pain with indwelling intrathecal pumps could resolve the issue that OP may be superior to opiates and may redirect research.


1992 ◽  
Vol 67 (03) ◽  
pp. 335-340 ◽  
Author(s):  
Fabian Chen ◽  
Edgar Haber ◽  
Gray R Matsueda

SummaryThe binding of radiolabeled monoclonal antifibrin antibody 59D8 (specific for fibrin but not fibrinogen) to a series of degraded fibrin clots showed that the availability of the Bβ(15-21) epitope (against which 59D8 had been raised) was inversely proportional to the extent of clot lysis. Examination of digest supernatants revealed that the Bβ(15-21) epitope was released from clots as a high molecular weight degradation product in the presence of calcium ions but that the generation of low molecular weight peptides occurred in the absence of calcium ions. To address the question of epitope accessibility, we compared levels of fibrin clot binding among four radioactively labeled antibodies: antifibrin monoclonal antibody 59D8, two antifibrinogen monoclonal antibodies that cross-reacted with fibrin, and an affinity-purified polyclonal antifibrinogen antibody. We expected that the antifibrinogen antibodies would show enhanced binding to clots in comparison with the antifibrin antibody. However, the epitope accessibility experiments showed that all four antibody preparations bound fibrin clots at comparable levels. Taken together, these studies demonstrated that one fibrin-specific epitope, Bβ(15-21), remains available on clots as they undergo degradation by plasmin and, importantly, that the epitope is not solubilized at a rate faster than the rate at which the clot is itself solubilized. The availability of the Bβ(15-21) epitope during the course of plasminolysis assures the potential utility of antifibrin antibodies such as 59D8 for detecting thrombi and targeting plasminogen activators.


1989 ◽  
Vol 15 (04) ◽  
pp. 440-463 ◽  
Author(s):  
Jawed Fareed ◽  
Jeanine Walenga ◽  
Debra Hoppensteadt ◽  
Adrienne Racanelli ◽  
Erwin Coyne

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