Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Sixty-eight methicillin-resistant Staphylococcus aureus strains were isolated from mastitis milk samples originating from 20 Belgian dairyherds. All these strains appeared to be representatives of one single strain which was probably of human origin. Evidence is presented indicating a rapid in vivo evolutionary change in this strain. The following characteristics were found to be variable: the production of beta haemolysin inversely connected with fibrinolysin (staphylokinase) activity; the production of lipase, enterotoxin B and delta haemolysin; the resistance to neomycin, chloramphenicol, tetracyclines, methicillin and spectinomycin associated with constitutive or inducible macrolide resistance.
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PMID:Epidemiology of methicillin-resistant Staphylococcus aureus in dairy herds. 12 47

Strains of Staphylococcus aureus that are lysed by typing phages 94 or 96, or by both phages, are usually resistant to lysis by other basic-set typing phages. They are, however, sensitive to several experimental phages and show a number of different lytic patterns when tested against these phages. These differences in susceptibility are due, in part, to immunity imposed by temperate phages carried by the different strains. Resistance to lysis by other basic-set phages was not due to prophage immunity, but to at least one restriction and modification system in such strains. Restrictionless mutants were isolated from one strain in several experiments. These showed an increased sensitivity to many basic-set phages. However, all of these mutants retained the ability to modify the phages to the characteristic "94, 96" specificity. Strains in the 94, 96 complex showed a remarkable homogeneity in biological traits. The majority were non-pigmented, and produced lipase, fibrinolysin, alpha and delta haemolysins and enterotoxin B. This homogeneity may well be a reflexion of the restriction and modification systems in these strains, that prevent the acquisition of genetic material from strains outside the complex. A new lytic group V is proposed for members of the 94, 96 complex.
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PMID:Properties of strains of Staphylococcus aureus in the 94, 96 complex. 14 Feb 44

The extracellular production of hyaluronidase and chondroitin sulfatase was demonstrated in all of the subspecies of Bacteroides fragilis tested with the exception of B. fragilis subsp. vulgatus. Elastase was found only in one strain of B. coagulans tested. This appears to be the first report of these enzyme activities in this genus. Additional enzymes found to be produced by certain members othis genus were fibrinolysin, penicillinase, lysozyme, lecithinase, deoxyribonuclease, phosphatase, protease, and lipase.
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PMID:Extracellular enzymes of the genus Bacteroides. 18 84

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

Production of 9 enzymatic activities of 527 strains freshly isolated from periodontal pockets in advancing periodontitis were investigated. Of these isolates, two strains showed lecithinase activity on egg yolk agar plate. Collagenase, plasmin and lipase were produced by 28 strains, 26 strains and 22 strains, respectively. Two lecithinase-producing strains were identified as Bacteroides intermedius. Nineteen strains of B. intermedius and 1 strain of Fusobacterium species produced lipase on egg yolk agar plate. All of the 28 collagenase-producing strains were B. gingivalis. B. gingivalis (20 strains) and non black-pigmented Bacteroides (6 strains) showed plasmin activity. These results indicate that Bacteroides species, mainly B. gingivalis and B. intermedius may exert an important influence on the exacerbation of the disease.
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PMID:[Distribution of enzymatically pathogenic bacteria from periodontal pocket in advancing periodontitis]. 196 47

A total of 5 Staphylococcus aureus strains from patients with postinfluenzal staphylococcal pneumonia, 7 from burn patients with staphylococcal pneumonia, and 21 from the nasopharynx of carriers were phenotypically characterized. All or most strains produced coagulase, clumping factor, DNase, thermostable DNase, protease, gelatinase, lipase, and pigment; the strains were low to moderate producers of extracellular protein A, fibrinolysin, and alpha-hemolysin. All strains were sensitive to mercury, half were sensitive to arsenate and cadmium, and 67 to 92% were resistant to penicillin. Differences between strains were not statistically significant. Cell surface hydrophobicity was determined by measuring percent adsorption to hexadecane. Hydrophobicity of postinfluenzal staphylococcal pneumonia strains was significantly lower than that of pneumonia strains from burn patients and carriers (P less than 0.005). Immunoblot experiments with sera immune to one clinical test strain allowed the separation of all strains into three groups based on probe-positive reactions with primarily four staphylococcal polypeptides (154,200, 130,000, 77,100, and 64,400 molecular weight). The difference in distribution of clinical and carrier strains was highly significant (P = 0.007).
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PMID:Characterization of clinical strains of Staphylococcus aureus associated with pneumonia. 301 27

Leukocidin from Fusobacterium necrophorum was produced in the diffusate of a dialysis culture. It was free from deoxyribonuclease, fibrinolysin, gelatinase, haemolysin, lipase, caseinase and endotoxin. The leukocidin had a molecular weight between 10,000 and 5,000 as estimated by membrane partition chromatography. It formed precipitin lines with anti-leukocidin-serum in double immunodiffusion tests. Mouse peritoneal cells were characteristically damaged by the leukocidin, as revealed by scanning electron microscopy. The damaged cells lost microvilli and suffered partial destruction of their cell membranes.
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PMID:Partial characterization of leukocidin from Fusobacterium necrophorum. 309 Aug 2

We have studied the binding and metabolism of 125I-labeled bovine lipoprotein lipase (LPL) by use of isolated, perfused rat livers. Our data suggest the presence of two types of binding sites, i.e., heparin-sensitive sites that bind primarily the catalytically active form of the lipase and are present at the endothelium in all blood vessels and heparin-insensitive sites that bind both active and inactive forms and are present only within the sinusoids. Forty minutes after uptake by the liver, approximately 50% of the LPL had lost its catalytic activity or been degraded. Three processes were evident: 1) colchicine-sensitive degradation to acid-soluble products, 2) partial proteolysis to fragments similar to those formed by limited digestion with trypsin or plasmin, and 3) a conformational change leading to loss of catalytic activity. Exogenous LPL bound in the liver caused a dramatic increase in the utilization of a perfused triacylglycerol emulsion (Intralipid), with rapid formation of free fatty acids and water-soluble metabolites. When the liver was flushed with heparin, it lost its ability to utilize the fat emulsion. Measurement of the hepatic extraction showed that rat livers take up 100-200 mU endogenous LPL per hour.
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PMID:Lipoprotein lipase uptake by the liver: localization, turnover, and metabolic role. 328 86

4-(2-Succinimidoethylthio) phenyl 4-guanidinobenzoate (E-3123) potently inhibited trypsin, plasmin and thrombin with IC50 values of 3.9 x 10(-8) M, 9.5 x 10(-7) M and 1.9 x 10(-6) M, respectively. Experimental acute pancreatitis was induced by injection of a mixture of trypsin and taurocholate into the pancreas in rats and rabbits or by an application of a closed duodenal loop in dogs. Intravenous infusion of E-3123 at 0.03-0.3 mg/kg in rats or at 0.3-3.0 mg/kg in rabbits reduced mortality after the induction of pancreatitis in a dose-dependent manner. Light microscopy of the pancreas in the E-3123-treated rabbits revealed marked decrease in cell necrosis and acinar cell vacuolation. Increase in plasma lipase activities associated with the progression of pancreatitis in rabbits was also reduced by the infusion of E-3123. In dogs with pancreatitis, increases in serum trypsin and lipase activities were significantly reduced by infusion of E-3123 at 1.0 and 3.0 mg/kg. The efficacies of E-3123 in the in vivo experiments were higher than those of nafamostat mesilate. These results show that E-3123 may possess suppressing effects on pathogenesis and development of acute pancreatitis.
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PMID:[Effects of E-3123, a new protease inhibitor, on several protease activities and on experimental acute pancreatitis]. 341 Mar 75

One hundred twenty-seven isolates of Aeromonas comprising the three currently recognizable species (A. hydrophila, A. sobria, and A. caviae) were evaluated for biochemical and exoenzymatic properties. Aeromonas species were generally (greater than 90%) characterized as gram-negative fermentative rods that were oxidase-, catalase-, and beta-galactosidase-positive, produced arginine dihydrolase, and failed to decarboxylate ornithine. More than 95% of all isolates tested failed to grow on 6.5% salt or thiosulfate-citrate bile salts agar and were resistant to the vibriostatic agent 0/129. Most Aeromonas species produced acid from hexoses while failing to ferment alcoholic sugars or trisaccharides. In exoenzymatic studies, Aeromonas species were uniformly found to produce several exoenzymes, including amylase, DNase, RNase, esterase, lipase, gelatinase, protease, fibrinolysin, and chitinase. Within the genus, a number of biochemical and enzymatic properties were found to be associated with one or more of the taxonomically recognizable species. These properties included glycoside utilization, Heiberg grouping based upon fermentation of arabinose, sucrose, and mannose, and the elaboration of several extracellular enzymes (elastase, hemolysin, lecithinase, phosphatase). In addition, phenotypic markers previously associated with enterotoxigenic Aeromonas isolates were almost exclusively found among A. hydrophila and A. sobria species, suggesting that these species are the major enteric pathogens.
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PMID:Biochemical and exoenzymatic properties of Aeromonas species. 388 8


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