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Human urine Urokinase

Urokinase (from human urine) [9039-53-6] Mr 53,000, [EC 3.4.21.31]. Crystn of this enzyme is induced at pH 5.0 to 5.3 (4") by careful addition of NaCl with gentle stirring until the soln becomes turbid (silky sheen). The NaCl concentration is increased gradually (over several days) until 98% of saturation is achieved whereby the urokinase crystallises as colourless thin brittle plates. It can be similarly recrystd to maximum specific activity [104K CTA units/mg of protein (Sherry et al. J Lab Clin Med 64 145 1964)]. [Lesuk et al. Science 147 880 1965 NMR Bogusky et al. Biochemistry 28 6728 1989.] It is a plasminogen activator [Gold et al. Biochem J 262 1989 ]. [Pg.573]

In 20 liters of human urine is dissolved 1,200 grams of sodium benzoate (6% weight by volume). The solution is acidified with aqueous hydrochloric acid (assay about 7.5% HCI) to a pH of 4.5 resulting in a heavy precipitation. This requires 10% of the original urine volume, or about 2 liters of aqueous hydrochloric acid. The suspension is stirred 20 minutes and is then allowed to stand for about 30 minutes. The mixture so obtained is filtered on a Buchner funnel that has been prepared with a precoat of benzoic acid crystals over filter paper. The filter cake is washed with a saturated benzoic acid solution, then sucked dry. The benzoic acid cake with the adsorbed urokinase weighs 2,060 grams. [Pg.1569]

Such clots—also known as emboli—present a serious hazard by their potential for blocking circulation of blood to vital organs. The considerable research devoted to agents that will lyse the fibrin in clots has led to the development of the clinically useful agent, uj-okinase. This drug is a fibrinolytic proteinaceous enzyme isolated from human urine. The difficulty involved in isolation of significant amounts and the antigenicity of urokinase and a related... [Pg.376]

Urokinase (extracted from human urine) Various... [Pg.346]

The ability of some component of human urine to dissolve fibrin clots was first noted in 1885. It was not until the 1950s, however, that the active substance was isolated and named urokinase. [Pg.350]

Urokinase utilized medically is generally purified directly from human urine. It binds to a range of adsorbents, such as silica gel and, especially, kaolin (hydrated aluminium silicate), which can be used initially to concentrate and partially purify the product. It may also be concentrated and partially purified by precipitation using sodium chloride, ammonium sulfate or ethanol as precipi-tants. [Pg.351]

Urokinase Urokinase is an enzyme that is extracted from human urine or kidney cells [46-55], which directly cleaves specific peptide bonds, in particular the Arg-560-Val-561 bond in the plasminogen molecule, thus transforming it into plasmin. It is used for the same indications as streptokinase. Synonyms of this drug are abbokinase and others. [Pg.331]

TNKase (Tenecteplase modified rtPA see Tenecteplase) Streptokinase (produced by Streptokinase haemolyticus) Urokinase (extracted from human urine)... [Pg.381]

Urokinase A protease which activates Human urine, or Treatment of venous... [Pg.420]

Urokinase (UK) was the first of the thrombolytic agents to appear in widespread use in the 1990s (20). UK is a naturally occurring thrombolytic produced by renal parenchyma and is therefore found in human urine. It has a plasma half-life of 15 minutes and when administered intravenously, it is rapidly removed from circulation by hepatic clearance. [Pg.571]

Urokinase is an enzyme obtained from human urine, that activates plasminogen. [Pg.362]

Urokinase is extracted from human urine or prepared from cultures of fetal kidney cells and does not seem to cause allergic reactions. [Pg.3404]

H2. Huber, K., Kirchheimer, J., and Binder, B. R., Rapid isolation of high molecular weight urokinase from native human urine. Thromb. Haemostas. 47, 197-202 (1982). [Pg.270]


See other pages where Human urine Urokinase is mentioned: [Pg.144]    [Pg.144]    [Pg.310]    [Pg.310]    [Pg.13]    [Pg.518]    [Pg.310]    [Pg.310]    [Pg.214]    [Pg.840]    [Pg.286]    [Pg.624]    [Pg.362]    [Pg.518]    [Pg.1569]    [Pg.310]    [Pg.310]    [Pg.1245]    [Pg.815]    [Pg.85]    [Pg.467]    [Pg.1256]    [Pg.1555]   


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