scholarly journals Biosynthesis of fibrinolytic agent urokinase by Enterococcus gallinarum isolated from sardine

2020 ◽  
Vol 19 (1) ◽  
pp. 213-225
Author(s):  
A. Nawaz ◽  
S.Q. Gillani ◽  
S.F. Tahir ◽  
K.A. Shah ◽  
S. Ashraf ◽  
...  
1973 ◽  
Vol 30 (01) ◽  
pp. 114-122
Author(s):  
C.R.M Prentice ◽  
K.M Rogers ◽  
G.P McNicol

SummaryThe pharmacological effect of a new preparation of urokinase (Leo) has been studied, both in vitro and in six patients suffering from thrombo-embolic disorders. It was a non-toxic, effective fibrinolytic agent if given in sufficient dosage. A regimen consisting of an initial dose of 7,200 ploug units per kg body weight, followed by hourly maintenance therapy with 3,600 ploug units per kg intravenously, gave satisfactory evidence of whole body fibrinolytic activity. The preparation had minor but insignificant thromboplastic activity both when assayed in the laboratory and when given to patients.


1982 ◽  
Vol 47 (03) ◽  
pp. 269-274 ◽  
Author(s):  
R A G Smith ◽  
R J Dupe ◽  
P D English ◽  
J Green

SummaryA derivative of human lys-plasmin in which the active site has been reversibly acylated (BRL 26920; p-anisoyl human lys-plasmin) has been examined as a fibrinolytic agent in a previously described rabbit model of venous thrombosis and shown to be significantly more active and less fibrinogenolytic than free plasmin. A p-anisoylated derivative of a streptokinase (SK)-activated plasmin preparation was significantly less fibrinogenolytic in vivo than the non-acylated enzyme. Acylation increased the fibrinolytic activity of preparations of SK-plasmin activator complexes. BRL 26921, the active site anisoylated derivative of the primary 2-chain SK-plasminogen complex was the most potent fibrinolytic agent studied. SK-Val442-plasminogen complexes, free or acylated, were biologically inactive in this model and confirm the essential nature of fibrin binding processes for effective thrombolysis in vivo.


2016 ◽  
Vol 5 (4) ◽  
pp. 325-336 ◽  
Author(s):  
Rakesh Soni ◽  
N.S. Bhatt ◽  
H.A. Modi ◽  
P.B. Acharya

1997 ◽  
Vol 119 (2) ◽  
pp. 175-181 ◽  
Author(s):  
Y. HIRAKATA ◽  
T. YAMAGUCHI ◽  
K. IZUMIKAWA ◽  
J. MATSUDA ◽  
K. TOMONO ◽  
...  

Glycopeptide resistance in enterococci is now a cause of clinical concern in the United States and Europe. However, details of vancomycin resistance in enterococci in Japan have been unknown. We measured minimum inhibitory concentrations (MICs) of various antimicrobial agents for a total of 218 clinical strains of enterococci isolated in our hospital in 1995–6 in addition to 15 strains with known genotypic markers of resistance. We also screened vancomycin resistance genes using a single step multiplex-PCR.In clinical isolates, only two strains of Enterococcus gallinarum were of intermediate resistance to vancomycin (MIC, 8 μg/ml), while the others were all susceptible. Glycopeptides (vancomycin and teicoplanin) and streptogramins (RP 58500 and RPR 106972) showed potent antimicrobial effects for the isolates. In addition, ampicillin was also potent for Enterococcus faecalis, while ampicillin, minocycline and gentamicin were potent for Enterococcus avium. No vanA or vanB genes were detected, while vanC1 and vanC23 genes were detected from two and four strains, respectively. Our results suggest that incidence of VRE in Japan may be estimated as still very low at this time.


2008 ◽  
Vol 57 (2) ◽  
pp. 244-245 ◽  
Author(s):  
Vânia Lúcia Carreira Merquior ◽  
Felipe Piedade Gonçalves Neves ◽  
Rachel Leite Ribeiro ◽  
Rafael Silva Duarte ◽  
Elizabeth de Andrade Marques ◽  
...  

A case of a post-surgical patient who developed a fatal bloodstream infection caused by high-level vancomycin-resistant Enterococcus gallinarum is reported. The isolate was found to carry both the vanC1 and vanA genes. This is the first report of an invasive infection associated with a vanA E. gallinarum isolate in Brazil.


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