Preparation and evaluation of nano-binary ethosomal dispersion for flufenamic acid

Author(s):  
Rana K. Muslim ◽  
Nidhal K. Maraie
1970 ◽  
Vol 23 (02) ◽  
pp. 202-210 ◽  
Author(s):  
R Bishop ◽  
H Ekert ◽  
G Gilchrist ◽  
E Shanbrom ◽  
L Fekete

SummaryA new fibrin plate technic for evaluating components of the fibrinolytic system has been developed. It provides quick, accurate, and easily interpreted results for the fibrinolytic profile. The standardized human plasminogen-free fibrin plates can be produced in bulk and stored for prolonged periods of time. A test specimen placed in a well punched in the buffered agarose gel diffuses into the agar and lyses the fibrin clot, forming a clear reaction zone. The zone diameter is directly proportional to the log of the percent concentration of available fibrinolytic enzyme in the specimen. The plates may be used to quantitate total plasminogen, and estimate available plasmin and active plasmin. A good correlation between results obtained using these fibrin plates and caseinolytic methods was found. Performance and interpretation of tests of fibrinolysis done on these new fibrin plates indicate that it may be the most sensitive technic available for clinical laboratory work.


1979 ◽  
Author(s):  
L Miles ◽  
J Burnier ◽  
M Verlander ◽  
M Goodman ◽  
A Kleiss ◽  
...  

Flu-HPA is one of a series of flufenamic acid derivations that enhances plasminogen-dependent clot lysis in vitro. Studies of possible mechanisms of action of Flu-HPA were undertaken. The influence of Flu-HPA on the inhibition of purified plasmin by purified PI was studied. PI activity was assessed by its inhibition of the clevage of the tripeptide S-2251 (H-D-Val-Leu-Lys-pNA) by plasmin. Flu-HPA was dissolved in DMF or in methonol and preincubated with PI before addition of plasmin. At Flu-HPA concentrations greater than 1mM and up to 60mM, the inhibitory activity of PI was totally lost. The inhibitory effect of normal human plasma on plasmin was also completely abolished at concentrations of Flu-HPA between 2.5 and 40mM. The effect of Flu-HPA on the inhibition of purified plasma kallikrein by purified CI-Inh was also studied. CI-Inh activity was measured by its inhibition of cleavage of the tripeptide Bz-Pro-Phe-Arg-pNA by kallikrein. When Flu-HPA, dissolved in DMF or in methonol, was preincubated with CI-Inh, a concentration dependent inhibition of CI-Inh activity was observed. CI-Inh activity was abolished by concentrations of Flu-HPA greater than 1mM. Flu-HPA also inhibited the activity of CI-Inh on purified Factor XIIa. These observations suggest that this flufenamic acid derivative may enhance fibrinolysis not only by inhibiting PI activity but also by decreasing the inactivation of plasminogen activators by CI-Inh.


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