Synthesis of Macromolecular Conjugates of a Urokinase Inhibitor: Amiloride

1999 ◽  
Vol 14 (2) ◽  
pp. 99-121 ◽  
Author(s):  
Janos Pató ◽  
Karel Ulbrich ◽  
Vladimir Subr ◽  
Peter Baker ◽  
Gábor Mezö ◽  
...  
1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.


2014 ◽  
Vol 32 (3) ◽  
pp. 1045-1054 ◽  
Author(s):  
Kara Lea Vine ◽  
Sergei Lobov ◽  
Vineesh Indira Chandran ◽  
Nathanial Lachlan Ewart Harris ◽  
Marie Ranson

1985 ◽  
Vol 230 (1) ◽  
pp. 109-116 ◽  
Author(s):  
H A Chapman ◽  
O L Stone

Human and mouse macrophages release a fibrinolytic inhibitor after stimulation by endotoxin in vitro. The released mouse inhibitor was indistinguishable in size by molecular-sieve chromatography from an intracellular form (approx. 50 kDa), and both inhibitors blocked urokinase directly as judged by a 125I-plasminogen conversion assay. The intracellular inhibitor was found mostly to dissociate from 125I-urokinase during sodium dodecyl sulphate/polyacrylamide-gel electrophoresis under reduced conditions, but a dodecyl sulphate-stable complex at 65-67 kDa was observed. Because of similarities in the reported size, stability and urokinase-binding properties of a placental urokinase inhibitor, the kinetic properties of the two inhibitors were compared. Under the reaction conditions employed (37 degrees C at pH7.4 in the presence of 0.2% Triton X-100), the association rate constants and equilibrium dissociation constants of the two inhibitors were indistinguishable, 3 × 10(5) M-1 × s-1 and 4 × 10(-10) M respectively. These data show that peritoneal macrophages contain a plasminogen-activator very similar to a previously recognized placental inhibitor. Although the inhibitor appears to be a trace protein in macrophages, placental macrophages may account for the accumulation of the inhibitor in placental tissue.


2016 ◽  
Vol 28 (1) ◽  
pp. 99-117
Author(s):  
Z. Stefanowicz ◽  
M. Sobczak ◽  
A. Piętniewicz ◽  
W.L. Kołodziejski

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