Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Necrotic materials most frequently found in leg ulcers, including crusts with fibrinogen, pus and blood clots, were exposed to solutions of streptokinase-streptodornase and stabilized crystalline trypsin respectively. The investigations were performed at the temperatures of 26 degrees and 33 degrees C, representing the extreme values of the temperature range found in leg ulcers (arteriosclerotic ulcers, stasis ulcers) and at the pH corresponding to that of the enzyme preparations in wet dressings. Streptokinase-streptodornase demonstrated in vitro a more potent proteolytic activity than crystalline trypsin on necroses, crusts of fibrinoid and purulent exudate, which were more rapidly and thoroughly broken up. Both enzyme preparations were, however, equally effective on three-day-old blood clots.
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PMID:Degradation and liquefaction effect of streptokinase-Streptodornase and stabilized trypsin on necroses, crusts of fibrinoid, purulent exudate and clotted blood from leg ulcers. 2 Nov 15

The release of beta-lysin, which followed the intravenous injection of antigen-antibody complexes, did not take place when these complexes were added to citrated whole blood but did occur in heparinized blood. beta-Lysin release in heparinized blood was inhibited by citrate but were reversed by the addition of calcium ions that implicated complement reactions. Fourteen different enzymes were added to platelet-rich plasma (PRP). Streptokinase, neuraminidase, papain, phospholipase C, sulfatase, and trypsin caused platelets to release significant quantities of beta-lysin, whereas elastase, phosphatase, protease, ribonuclease A, hyaluronidase, lipase, and pepsin caused little or no increase in the plasma beta-lysin concentration. One enzyme, fibrinolysin, inactivated beta-lysin faster than it was released. The enzyme-induced release of beta-lysin from PRP was often accompanied by a reduction in the number of platelets. The intravenous injection of streptokinase, neuraminidase, and sulfatase caused in vivo releases of beta-lysin into the plasma. The platelet-aggregating substances collagen, arachidonic acid, and adenosine 5'-diphosphate caused beta-lysin to be released from PRP. The platelet-aggregating substances L-epinephrine, zymosan, fibrinogen, reserpine, and serotonin caused little or no release of beta-lysin from platelets. The results of this study indicate that the release of beta-lysin during antigen-antibody-complement reactions, blood coagulation, phagocytosis, and inflammation could be enzyme mediated.
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PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4

The catabolic pathways of streptokinase, plasmin, and activator complex prepared with human plasminogen were studied in mice. (125)I-streptokinase clearance occurred in the liver and was 50% complete in 15 min. Incubation with mouse plasma had no effect on the streptokinase clearance rate. Complexes of plasmin and alpha(2)-plasmin inhibitor were eliminated from the plasma by a specific and saturable pathway. Competition experiments demonstrated that this pathway is responsible for the clearance of injected plasmin. Streptokinase-plasminogen activator complex formed with either (125)I-plasminogen or (125)I-streptokinase cleared in the liver at a significantly faster rate than either of the uncomplexed proteins (50% clearance in <3 min). Streptokinase incubated with human plasma also demonstrated this accelerated clearance. p-Nitrophenyl-p'-guanidinobenzoate-HCl or pancreatic trypsin inhibitor-treated complex cleared slowly compared with untreated complex independent of which protein was radiolabeled. Significant competition for clearance was demonstrated between alpha(2)-macroglobulin-trypsin and activator complex only when the plasmin(ogen) was the radiolabeled moiety. Large molar excesses of alpha(2)-plasmin inhibitor-plasmin failed to retard the clearance of activator complex. Hepatic binding of streptokinase-plasmin, in liver perfusion experiments, was dependent upon prior incubation with plasma (8-10% uptake compared to a background of approximately 2.5%). Substitution of human alpha(2)-macroglobulin for plasma also resulted in binding when the incubation was performed for 10 min at 37 degrees C (7.5%). Electrophoresis experiments confirmed the transfer of 0.8 mol plasmin/mol alpha(2)-macroglobulin when activator complex was incubated at 37 degrees C with alpha(2)-macroglobulin for 40 min. Streptokinase transfer from activator complex to alpha(2)-macroglobulin was negligible. The in vivo clearance of activator complex is proposed to involve active attack of the complex on the alpha(2)-macroglobulin "bait region," resulting in facilitated plasmin transfer. Dissociated streptokinase is rapidly bound and cleared by sites in the liver.
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PMID:Catabolic pathways for streptokinase, plasmin, and streptokinase activator complex in mice. In vivo reaction of plasminogen activator with alpha 2-macroglobulin. 617 57

The complete amino acid sequence of streptokinase has been determined by automated Edman degradation of its cyanogen bromide and proteolytic fragments. The protein consists of 415 amino acid residues. Sequence microheterogeneity was found at two positions. The NH2-terminal 245 residues of streptokinase are homologous to the sequences of several serine proteases including bovine trypsin and Streptomyces griseus proteases A and B. The sequence alignment suggests that the active-site histidine-57 has changed to a glycine in streptokinase. The other active-site residues, aspartyl-102 and serine-195, are, however, present at the expected positions. Streptokinase also contains internal sequence homology between the NH2-terminal 173 residues and a COOH-terminal 162-residue region between residues 254 and 415. Moderate homology in predicted secondary structures also exists between these two regions. Although streptokinase is not a protease, these observations suggest that it has evolved from a serine protease by gene duplication and fusion. A COOH-terminal region of about 80 residues is apparently deleted from the second half of the duplicated structures. These observations further suggest that the three-dimensional structure of streptokinase likely contains two independently folded domains, each homologous to serine proteases.
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PMID:Complete amino acid sequence of streptokinase and its homology with serine proteases. 676 Aug 91

The cleansing effects on pus and debris of streptokinase-streptodornase and of stabilized crystalline trypsin were compared in 40 patients (12 males, 28 females) with necrotic varicose or arteriosclerotic leg ulcers. Both preparations produced significant partial or total cleansing of the ulcers of necrotic material, and both enhanced the granulation and epithelialization of most of the ulcers. Streptokinase-streptodornase was significantly more effective in removing freshly formed damp and smearing pus and debris. Neither preparation prevented the formation of or removed very deep adherent necrotic areas, especially in arteriosclerotic leg ulcers. Trypsin caused significantly more pain than streptokinase-streptodornase during the treatment period and on changing dressings. Both enzymes indirectly reduced the bacterial flora of the ulcers, probably by removal of necrotic wet material.
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PMID:Cleansing properties of stabilized trypsin and streptokinase-streptodornase in necrotic leg ulcers. 687 40

Prevailing fibrin-formation in the pleural cavity entails hypoactivity of trypsin-like proteinases and a high inhibitory potential in the serum and pleural exudate. Streptokinase preparations appeared an effective means of pharmacological pulmonary decortication in patients with high pleural levels of plasminogen. The authors obtained higher efficacy of conservative therapy for pyothorax when they used a specially designed technique of intrapleural administration of streptokinase-activated fresh frozen plasma of the same group. The outcomes of the disease were also improved noticeably.
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PMID:[The use of streptokinase preparations in pleural empyema and pyopneumothorax]. 820 57

Streptokinase (SK) exerts its thrombolytic effect by activating plasminogen (PG) indirectly, after the formation of an equimolar complex with either PG or plasmin (PN). The location and nature of the PG/PN-binding sites in SK have been explored using limited proteolysis with immobilized trypsin. Employing Western blotting with radiolabeled PG after SDS-PAGE of total tryptic digest, three fragments of MW 7 kD, 19 kD and 31 kD were found to possess PG-binding ability. Each of these fragments was then isolated by reverse phase HPLC and characterised with respect to its sequence, as well as its PG-binding properties by ELISA. These analyses revealed that in addition to a PG-binding site in the region 143-293 reported recently in the literature, there is another distinct, high-affinity and independent PG-binding site, located in the N-terminal region (residues 1-59) of SK. Using a synthetic peptide, the N-terminally located PG-binding-site has been further localised to the region 37-51 of SK. Further, we demonstrate that the PG-binding of this peptide is not mediated through the lysine-binding sites ("Kringles") of PG. This stretch contains a short sequence (LTSRPA) that is also present in the PG-binding domain of human fibronectin.
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PMID:Streptokinase contains two independent plasminogen-binding sites. 855 83