DETERMINATION OF INHIBITORS OF UROKINASEACTIVATED FIBRINOLYTIC ENZYME SYSTEM BY MEANS OF GEL FILTRATION IN HUMAN SERUM

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

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The Kidney and Fibrinolysis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654207 ◽

1970 ◽

Vol 24 (01/02) ◽

pp. 026-032 ◽

Cited By ~ 2

Author(s):

N. A Marsh

Keyword(s):

Molecular Weight ◽

Plasminogen Activator ◽

Enzyme System ◽

Normal Animal ◽

Fibrinolytic Enzyme ◽

The Other ◽

Exclusion Chromatography ◽

Normal Urine ◽

Renal Origin ◽

Molecular Exclusion Chromatography

SummaryMolecular exclusion chromatography was performed on samples of urine from normal and aminonucleoside nephrotic rats. Normal urine contained 2 peaks of urokinase activity, one having a molecular weight of 22,000 and the other around 200,000. Nephrotic urine contained three peaks of activity with MW’s 126,000, 60,000 and 30,000. Plasma activator determined from euglobulin precipitate had a MW. in excess of 200,000. The results indicate that in the normal animal, plasma plasminogen activator does not escape into the urine in substantial quantities but under the conditions of extreme proteinuria there may be some loss through the kidney. The alteration in urokinase output in nephrotic animals indicates a greatly disordered renal fibrinolytic enzyme system.The findings of this study largely support the hypothesis that plasma plasminogen activator of renal origin and urinary plasminogen activator (urokinase) are different molecular species.

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The Different Forms of Antithrombin III in Serum

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651855 ◽

1977 ◽

Vol 38 (02) ◽

pp. 0494-0503 ◽

Cited By ~ 18

Author(s):

D. S Pepper ◽

D Banhegyi ◽

J. D Cash

Keyword(s):

Molecular Weight ◽

Affinity Chromatography ◽

Human Serum ◽

Degradation Product ◽

Antithrombin Iii ◽

Gel Filtration ◽

Free Form ◽

Polymeric Form ◽

At Iii ◽

Human Thrombin

SummaryAntithrombin III (AT III) complexes were isolated from human serum by affinity chromatography and gel filtration. In the first step of the preparation, using heparin-agarose chromatography, we observed that the complexed form of AT III bound less strongly to the gel than the free form and that about half of the AT III was free. With further purification a 2.5 × 105 molecular weight complex was isolated. Using 125I labelled human thrombin, this complex was radioactive indicating the presence of thrombin. Only in a synthetic thrombin-AT III system was a 9 × 104 molecular weight complex detected, but not in serum. These facts suggest that in serum AT III complexes may exist in a polymeric form. Also, an AT III antigen derived from the original AT III molecule, but not complexed, was isolated which may be a degradation product.Abbreviations used: AT-III, antithrombin III. Hepes, N-2-Hydroxyethylpiperazine-N-2-Ethanesulphonic acid.

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Arterio-Venous Differences in the Components of the Fibrinolytic Enzyme System

Thrombosis and Haemostasis ◽

10.1055/s-0038-1655624 ◽

1966 ◽

Vol 16 (01/02) ◽

pp. 032-037 ◽

Cited By ~ 5

Author(s):

D Ogston ◽

C. M Ogston ◽

N. B Bennett

Keyword(s):

Plasminogen Activator ◽

Enzyme System ◽

Venous Blood ◽

Fibrinolytic Enzyme ◽

Blood Levels ◽

Activator Concentration ◽

Blood Samples ◽

Arterial Blood ◽

Male Subjects

Summary1. The concentration of the major components of the fibrinolytic enzyme system was compared in venous and arterial blood samples from male subjects.2. The plasminogen activator concentration was higher in venous blood and the arterio-venous difference increased as its concentration rose, but the ratio of the arterial to venous level remained constant.3. No arterio-venous difference was found for anti-urokinase activity, antiplasmin, plasminogen and fibrinogen.4. It is concluded that venous blood determinations of the components of the fibrinolytic enzyme system reflect satisfactorily arterial blood levels.

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