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 quantitative estimation of soluble fibrin monomer complexes (SFMC) was applied to evaluate the state of hypercoagulability during pregnancy and delivery. Blood samples from 67 healthy primi and multiparae, 6 to 40 weeks pregnant, and from a group of 8 women in labour and after delivery of the placenta were examined. Fibrinogen and SFMC were precipitated from plasma by precipitation with beta-alanine. Gel filtration (4% agarose) of the redissolved precipitate resulted in a separation of SFMC and fibrinogen. This enabled a quantitative estimation of the SFMC concentration (with-in assay precision: coefficient of variation=8%). The % amount SFMC of the total fibrinogen content increased from 2.6 +/- 0.4 to 4.9 +/- 1.3% (mean and standard deviation) to week 40 of pregnancy. During delivery an additional statistically significant increase occurred. Chain analysis of SFMC showed a decreased amount of alpha-chain indicating plasmin activity. gamma-gamma-dimers as residuals of intermolecular covalent bonding were not observed. The quantitative estimation of SFMC during pregnancy and delivery demonstrates that a state of hypercoagulability during gestation can be evaluated by measuring the catabolic products of fibrinogen. This may lead to a differentiation from severe intravascular coagulation and to an early diagnosis of thromboembolic disease or consumption coagulopathy.
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PMID:[Estimation of soluble fibrin monomer complexes for evaluation of hypercoagulability during pregnancy and delivery (author's transl)]. 121 64

Fibrinogen was purified from fresh citrated human plasma by precipitation with beta-alanine in the presence of citrate and protease inhibitors. From this material, fractions corresponding to the HMW (high molecular weight), LMW and LMW' fibrinogen fractions of plasma were obtained by step-wise precipitation with ammonium sulfate. Electrophoresis revealed that HMW was contaminated with 4% LMW, LMW was contaminated with 6% HMW, and the LMW'-fraction was a mixture of LMW' (50%), LMW (20%) and two derivatives of intermediate m.w.. The HMW fraction (mw. 340 000) contained intact Aa-chains, while the molecular weight of LMW was reduced to 305 000 and that of LMW' to 270 000 due to proteolysis of the -COOH terminal end of one (LMW) or both (LMW') Aa-chains. The clottability of HMW was 98%, of LMW 92% and of LMW' about 80%. Thrombin clotting times (1 NIH U/ml) were 14", 20" and 25" resp. These differences were highly accentuated when clotting was performed with reptilase (14", 38" and 120"). Contamination with soluble fibrin was less than 2% and the contents of fibronectin and AT-III were low. No thrombin or plasmin activity was generated upon 24 hours incubation at +4 degrees C as evidenced by increased content of fibrinopeptide-A and fragment Bb-15-42 resp.
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PMID:Purification and characterization of 3 fibrinogens with different molecular weights obtained from normal human plasma. 398 97

Both soluble and insoluble fibrin stimulate the tissue-type plasminogen activator-catalysed conversion of plasminogen to plasmin. Whether fibrinogen can exert a similar effect has been a controversial issue. The present investigation shows that while fibrinogen purified by beta-alanine precipitation does not stimulate the tissue-type plasminogen activator-catalysed plasminogen activation, fibrinogen which has been either lyophilized or stripped of bound Ca2+ ions by EDTA chelation, stimulates this reaction. The data indicate that such procedures alter the molecular conformation of fibrinogen, and expose stimulatory sites which are hidden in the native fibrinogen molecule. These results may explain previous findings concerning the capacity of fibrinogen as a stimulator of the tissue-type plasminogen activator-catalysed plasminogen activation. Since even slight alteration of the molecular structure of fibrinogen leads to an increase in the tissue-type plasminogen activator stimulation, the authors suggest that this can be used to test if the fibrinogen is in a native state.
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PMID:Freeze-dried fibrinogen or fibrinogen in EDTA stimulate the tissue-type plasminogen activator-catalysed conversion of plasminogen to plasmin. 784 14