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

Histones form insoluble complexes with heparin and neutralize its anticoagulant action. The plasmin degradation products of histones do not possess these properties. Plasmin also digests histones in complexes with heparin. Breakdown of the histones in these complexes causes release of heparin from them.
Acta Haematol Pol 1979 Oct
PMID:[Histone-heparin complexes]. 4 65

The activation of human plasminogen by a highly purified staphylokinase was investigated using casein or an active site titrant (p-nitrophenyl-p-guanidinobenzoate, NPGB) as a substrate. The reaction rate was time dependent, showing a pronounced lag period with either substrate. Saturation curve estimated from the caseinolytic assay was sigmoid, but changed to quasi-hyperbolic in the presence of pre-formed human plasmin. With NPGB, the extent of plasminogen conversion into esterolytic plasmin was directly proportional to staphylokinase concentration, and the saturation point was reached when the molar concentration of staphylokinase equaled that of plasminogen. It is concluded that staphylokinase acts stoichiometrically, forms an equimolar complex with plasminogen, and thus is not an enzyme but a modifier. Staphylokinase-activated plasminogen exhibits properties of a hysteretic enzyme.
Acta Biochim Pol 1975
PMID:The activation by staphylokinase of human plasminogen. 13 46

Protamine-heparin complexes have a considerable resistance to physical factors of the environment such as a high ion strength and acid or alkaline pH. Free protamine is digested by plasmin giving products with a greatly decreased ability to form complexes with heparin and lower antiheparin action. Bound protamine, on the other hand, is resistant to the action of plasmin as a result of which the enzyme does not release heparin from the complexes.
Acta Haematol Pol
PMID:[Properties of protamine-heparin complexes]. 15 86

Latent collagenase has been isolated in pure form from the rheumatoid synovial fluid. The final preparation, activated by trypsin, yielded a collagenase of specific activity 2,227 units/mg. Electrophoresis in sodium dodecyl sulfate polyacrylamide gels revealed a protein doublet of 54 and 50 kDa. Trypsin or HgCl2 activation resulted in disappearance of the doublet and emergence of a new doublet of 47 and 43 kDa. The latent collagenase could also be activated by leucocyte cathepsin G or plasmin. Neither the latent nor the active collagenase from synovial fluid showed any cross-reactivity with the antibodies against leucocyte collagenase. The trypsin activated collagenase degraded collagen type I, II, III giving typical cleavage products but did not degrade type IV and V collagen.
Acta Biochim Pol 1990
PMID:Some properties of latent collagenase from human synovial fluid. 196 84

Duck fibrinogen (Mr 320 000) treated with streptokinase-activated human plasminogen in the presence of calcium ions was hydrolysed to terminal core fragments D and E. They were isolated from the digest by: (1) ion-exchange chromatography on DEAE-cellulose, (2) gel filtration on Sephadex G-100, and (3) affinity chromatography with the use of fibrin monomers coupled to CNBr-activated Sepharose. When the native D fragment, D1 was additionally digested by plasmin in the presence of EDTA, more degraded forms D2 and D3 appeared. Molecular weight of D1, D2, D3 and E estimated on SDS-polyacrylamide gel electrophoresis is 100 000, 89 000, 80 000 and 50 000, respectively. It was found that after reduction with 2-mercaptoethanol the fragments D1 and D3 consisted each of three polypeptide chains: alpha, beta, gamma: the gamma-chain of D3 remnant was more degraded (Mr 24 000) as compared with the gamma-chain of D1 remnant (Mr 42 000). Polymerization of both duck and pig fibrin monomers was inhibited by fragments D1 but not by D3.
Acta Biochim Pol 1985
PMID:Terminal plasmin degradation products D and E of duck fibrinogen and their effect on polymerization of fibrin. 403 48

No effect of fibrinogen degradation products on specific binding of [3H]spiroperidol and [3H]ADTN was observed. Low molecular weight peptides derived from fibrinogen degradation by plasmin (FDP) increase the motor activity of rats [7] augment apomorphine- and amphetamine-induced stereotypy and diminish haloperidol catalepsy [2]. It has been suggested that FDP interact with central dopamine receptor [2]. Taking the above considerations into account it was decided to investigate the effect of FDP on specific binding of [3H] spiroperidol and 2-amino-6,7-dihydroxy-1,2,3,4-tetrahydronaphthalene ([3H]ADTN).
Pol J Pharmacol Pharm 1983
PMID:Lack of effects of fibrinogen degradation products on specific binding of [3H]spiroperidol and [3H]ADTN. 688 86

Methods for measuring antigen and activity of plasminogen activators (t-PA, u-PA), plasminogen activator inhibitors (PAI-1, PAI-2) and their complex have been improved in the past few years, but few comparative data are available and they should be standardized. In particular the commercial kits for determination of PAI-1 activity seem to be not accurate for the measurement of PAI-1 in plasma. The amount of generated plasmin can be measured as plasmin-alpha-2-antiplasmin complex (PAP). There are also some new tests which could differentiate between fibrinogenolysis (FgDP) and fibrinolysis (FnDP, D-dimer) as between primary and secondary activation of fibrinolysis (B beta 15-42 peptide). Normal D-dimer plasma concentration allows for the ruling out of venous thromboembolism with high probability, but the specificity of this tests is poor.
Acta Haematol Pol 1995
PMID:[Progress in the detection of intravascular activation of fibrinolysis]. 774 60

Five new dipeptides containing epsilon-aminocaproic acid were synthesized. All dipeptides markedly inhibit fibrinolytic activity of plasmin but only in low concentration (0.0002M). In higher concentration fibrinolytic activity was observed. Activity of dipeptides containing epsilon-aminocaproic acid, which antifibrinolytic activity is known, was tested on plasmin, thrombin, urokinase and euglobulin fraction using synthetic substrates.
Acta Pol Pharm 1994
PMID:Synthesis and activity of dipeptides containing epsilon-aminocaproic acid. 776

The aim of this study was to compare the secretory response of the vascular wall in vivo to DDAVP (i.v. 0.3 microgram/kg, 30 min) and to venous occlusion (VO, 20 min) in control healthy subjects, patients with von Willebrand's disease type I (vWd I) and patients with von Willebrand's disease type III (vWd III). In controls (n = 10) and vWd I (n = 12), DDAVP induced a 2 to 3-fold rise in plasma von Willebrand factor antigen (vWf: Ag), factor VIII coagulant activity (VIII: C) and tissue--type plasminogen activator antigen (t-PA:Ag). VO was less effective in increasing vWf: Ag and VIII:C but produced a greater rise in t-PA:Ag. Large increments (over 10-fold) were observed in plasmin-alpha 2-antiplasmin complexes following both stimuli. In vWd III (n = 10), DDAVP and VO failed to increase vWf:Ag, VIII:C and t-PA:Ag. No significant changes in plasmin-alpha 2-antiplasmin complexes were observed in this group. Moreover, the baseline t-PA:Ag values were significantly lower in vWd III (2.17 +/- 1.13 ng/ml) than in controls (4.84 +/- 1.97 ng/ml, p < 0.001). A significant increase in urokinase--type plasminogen activator antigen (u-PA:Ag) was found only in controls after VO. Neither controls nor patients with vWd showed any changes in plasma fibronectin levels following DDAVP. The low t-PA:Ag results and the abnormal fibrinolytic response to DDAVP and VO in patients with severe (type III) vWd indicate that their endothelial cell abnormality is more extensive than the defect in the synthesis or release of vWf.
Acta Haematol Pol 1994
PMID:Secretory response of the vessel wall to DDAVP and venous occlusion in von Willebrand's disease. 799 99

The pre- and postoperative activity was studied of antithrombin III (AT III) and alpha 2-antiplasmin (alpha 2-AP) in blood of 40 patients subjected to transurethral prostatic electroresection due to benign prostatic hyperplasia (BPH). For comparison of the obtained results a control group was formed from patients with other diseases of the genitourinary system with exception of neoplasms. The activity of AT III and alpha 2-AP before the operation was similar to that in the control group. Intraoperatively (day 0) and on the first day after the operation, a statistically significantly lower activity of AT III and alpha 2-AP was found in the patients with BPH in relation to the initial value as well as to the control group. On day 5 after the operation, normalization of AT III and alpha 2-AP activity was found. During operations of the prostate a release occurs of thromboplastins and plasminogen activators initiating the activation of blood clotting and fibrinolysis. The decrease of activity of AT III and alpha 2-AP could be caused by AT III and alpha 2-AP use-up in the process of inhibition of the created thrombin and plasmin.
Pol Tyg Lek 1996 Feb
PMID:[Antithrombin III and alpha 2-antiplasmin in blood of patients operated on for benign prostatic hyperplasia]. 875 35


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