Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.73 (urokinase-type plasminogen activator)
 10,685 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two genetically engineered E. coli strains L+ and CAG+ possessing the ability to produce the enzyme Pro-urokinase and showing additionally ampicillin resistance, and wild-strains L- and CAG-, were characterized using 328 physiological tests. Their test profiles were compared with those of 30 clinical and nonclinical E. coli isolates. This biotyping made a differentiation and recognition of the genetically manipulated strains possible. It also allowed distinguishing them from the other tested isolates. The genetically engineered strains showed a narrower activity spectrum compared with their wild-strains. However, based on differentiating characteristics, all strains could be clearly biochemically identified as E. coli. Under different laboratory test conditions (organic load, pH, salt content, temperature), the E. coli strains showed no striking features or peculiarities with respect to their survival compared to data from literature. However, low pH (pH less than 5), high salt content (greater than 7%) as well as low (less than 8 degrees C) and high (greater than 37 degrees C) incubation temperatures clearly reduced their ability to survive. Apart from a few exceptions (e.g. survival of strain L+ at 44 degrees C and pH 7 with high cell densities), the survival of the genetically engineered strains corresponded to that of the control and wild-strains. Both CAG strains, especially the genetically manipulated strain CAG+, showed in many cases reduced viability compared with the other strains.
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PMID:[Survival ability of genetically engineered strains of Escherichia coli. 1. Physiological characterization and the effect of different physiochemical conditions]. 188 76

The polymerized beta-lactam antibiotic ampicillin inhibits the proteolytic activity of human plasmin upon 125I-labeled fibrin clots. The inhibition is dose-dependent, with half-maximal inhibition occurring at 1.25 mM of the polymerized antibiotic. Polymerized ampicillin also inhibits binding of plasmin to fibrin, and 38% inhibition of binding occurs at 10 mM of the antibiotic. Furthermore, polymerized ampicillin inhibits the activation of plasminogen by either urokinase-like plasminogen activator (uPA) or tissue type-plasminogen activator (tPA). At 7.5 mM of polymerized ampicillin, the uPA-mediated plasminogen activation is suppressed by 94%, and half-maximal inhibition is obtained at 0.66 mM. The direct activity of uPA on the chromogenic substrate L-pyroglutamyl-glycyl-L-arginine p-nitroanilide hydrochloride (S-2444) is unaffected by polymerized ampicillin levels of up to 10 mM. The inhibitory effects of the polymerized antibiotic on the activation of plasminogen by both uPA and tPA is totally abolished in presence of fibrin. These interactions may serve as a novel model for ligands that enhance the clot-specificity of thrombolytic agents.
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PMID:Inhibition of plasminogen activation by polymerized ampicillin. 783 83