Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The relationship between factor VIII (AHF) procoagulant activity and factor VIII-related antigen were examined in patients with disseminated intravascular coagulation (DIC), pulmonary embolism (PE), and coronary artery disease with or without myocardial infarction (MI). It was found that 13 of 13 patients with DIC, 17 of 17 patients with PE, and 10 of 12 patients with MI possessed a significantly elevated factor VIII-related antigen to factor VIII activity ratio (VIII-ratio). The VIII-ratio returned to normal in each of 2 patients with DIC and 1 paitent with PE after treatment with heparin, heparin and alpha-amino-caproic acid, and heparin and coumadin respectively. In contrast, the VIII-ratio was slightly elevated only in 1 of 15 patients with coronary artery insufficiency without MI. In in vitro studies, after treatment of plasma with thrombin or plasmin, factor VIII activity was lost, whereas the amount of factor VIII-related antigen remained the same or was even increased when measured by agarose quantitative immunoelectrophoresis. These observations have led us to conclude that an elevated VIII-ratio is a very sensitive indicator of intravascular coagulation.
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PMID:In vivo and in vitro effects of thrombin and plasmin on human factor VIII (AHF). 13 71

Partially purified human antihemophilic factor (AHF, factor VIII), when treated with high concentrations of salt, has been shown to dissociate into two components: one, of relatively low molecular weight, possesses procoagulant activity, and the other, of higher molecular weight, forms precipitates with heterologous antiserum against AHF and supports ristocetin-induced platelet aggregation. The ease of separation suggests that the two components in the native state might be held together by noncovalent bonds. Earlier observations do not exclude the possibility that the subunits may be covalently bonded in nature but might be severed by plasma proteolytic enzymes during laboratory manipulation. The issue was examined by preparing partially purified AHF from fresh human plasma in the presence of protease inhibitors, including benzamidine, soybean trypsin inhibitor, epsilon-aminocaproic acid, heparin, and hirudin. Under these conditons, gel filtration in the presence of 0.25 M calcium chloride and 0.001 M benzamidine resulted in its separation into two components, having properties identical to those separated in the absence of these protease inhibitors. The inhibitor mixture blocked generation and action of streptokinase- and kaolin-activated plasmin from plasma, and protected both plasma AHF and partially purified AHF from the action of thrombin. Surface-induced activation of PTA (factor XI) was partially inhibited, and that of Christmas factor (factor IX) was completely inhibited. This observation provides further evidence that in the native state the high- and low-molecular-weight components of preparations of antihemophilic factor are held together by noncovalent bonds.
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PMID:Evidence that functional subunits of antihemophilic factor (Factor VIII) are linked by noncovalent bonds. 94 7

Four large-scale batches of Antihemophilic Factor (AHF, factor VIII) were prepared from plasma derived from 4 to 6-day-old blood applying a method developed for preparation of AHF from fresh frozen plasma. The AHF product was 6 to 9-fold concentrated over plasma with 7 to 10-fold purification and a recovery of 100 to 140 factor VIII units per liter of starting plasma. In terms of purity and yield, this is about half that of AHF obtained from fresh frozen plasma. The AHF concentrate was free of detectable thrombin and plasmin and the solubility of the dry product was comparable to that of the product derived from fresh plasma but the hemoglobin content was slightly increased. After further fractionation with polyethylene glycol (PEG 4000), a highly soluble AHF product 100-fold purified, and 30-fold concentrated, was obtained with 60% factor VIII recovery, which corresponds to a final yield of 60 to 85 factor VIII units per liter of starting plasma.
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PMID:Preparation of antihemophilic factor from indated plasma. 95 29

A patient with Weber-Christian disease (syn. nodular nonsuppurative panniculitis) is reported. The generalized cellular destruction in this patient resulted in liberation of proteolytic enzymes into the circulation, which led to multiple haemostatic disturbances with haemorrhagic diathesis. The most prominent haemostatic defects were thrombocytopenia with a normal life span of isologous platelets, high levels of AHF-related antigen, hypofibronigenaemia with short fibrinogen survival, low levels of Factor XIII (fibrin stabilizing factor = FSF) and increased amounts of fibrin/fibrinogen degradation products (FDP). Proteolytic enzymes, other than thrombin and plasmin which especially degrade Factor XIII and fibrongen, derived from destroyed cells (probably leukocytes) seem to have been involved in the pathogenesis of the bleeding disorder in this patient.
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PMID:Generalized proteolysis in a young woman with Weber-Christian disease (nodular nonsuppurative panniculitis). 121 32