Detection of parvovirus DNA in human serum using biotinylated RNA hybridisation probes

ZusammenfassungNach tierexperimentellen Voruntersuchungen wurde die Placentographie mit trägerfreiem 113Inm -HSA als klinische Methode eingeführt. Vor Amniocentesen und bei Verdacht auf Placenta praevia werden Placentographien geschrieben. Den Schwangeren wird eine Aktivität von 500 μCi in die Cubitalvene injiziert. Die der Aktivität entsprechende Indiummenge ist kleiner als 0,1 ng. Die fetale Strahlenbelastung liegt unter lOmrad. Bei Anwendung von 113Inm-HSA entfällt eine Blockade der mütterlichen und fetalen Schilddrüsen. Die genaue Abgrenzung einer Placenta praevia wird nicht durch eine Blasenaktivität beeinträchtigt.Es wurden bisher 19 Placentalokalisationen durchgeführt. In allen Fällen konnte der Placentasitz eindeutig festgestellt werden. Bedingt durch die lange Liegezeit beim Aufnehmen eines Szintigramms kam es in zwei Fällen zu einem Vena-Cava-Kompressions-Syndrom. Zur Verhinderung dieser klinischen Zwischenfälle werden inzwischen Placentographien mit der Anger-Kamera aufgenommen. Mit Hilfe des divergierenden Kollimators konnte der gesamte Abdominalbereich erfaßt werden. Die Aufnahmezeit konnte auf 7 — 10 Minuten verkürzt werden. Die intravenöse injizierte Aktivität betrug bei dieser Methode ebenfalls 500 μCi. Der diagnostische Aussagewert der Kamerabilder ist szintigraphischen Aufnahmen gleichwertig.

Download Full-text

Studies on an Inhibitor of Plasminogen Activation in Human Serum

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649120 ◽

1973 ◽

Vol 30 (02) ◽

pp. 414-424 ◽

Cited By ~ 20

Author(s):

Ulla Hedner

Keyword(s):

Ion Exchange ◽

Human Serum ◽

Antithrombin Iii ◽

Gel Filtration ◽

Ion Exchange Chromatography ◽

Exchange Chromatography ◽

Specific Adsorption ◽

Partial Purification ◽

Plasminogen Activation ◽

Preparative Electrophoresis

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.

Download Full-text

Human Blood Serum Rich in Factor V

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654241 ◽

1970 ◽

Vol 24 (03/04) ◽

pp. 334-337 ◽

Cited By ~ 1

Author(s):

R Honorato

Keyword(s):

Blood Serum ◽

Human Serum ◽

Human Blood ◽

Human Blood Serum ◽

Factor V ◽

The Stability

Summary1. A technique to obtain human serum rich in factor V is described.2. Calcium increases the stability of factor V in the serum.

Download Full-text

On the Behaviour of a Human Serum Proactivator Reacting with Streptokinase during Artificial Activation of the Fibrinolytic System

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654581 ◽

1961 ◽

Vol 06 (03) ◽

pp. 498-503 ◽

Cited By ~ 1

Author(s):

W Doleschel ◽

W Auerswald

Keyword(s):

Human Serum ◽

Fibrinolytic System ◽

Spontaneous Activation ◽

Significant Change ◽

Artificial Activation ◽

Activator System

SummaryDuring “spontaneous” activation of a human euglobulin preparation in suitably spaced samples — while plasminogen became progressively converted into piasmin — the proactivator content was tested by addition of equal amounts of streptokinase and evaluation of the lytic activities on heated and normal bovine fibrin plates. Indepedently of the decreasing content of plasminogen the proactivator which could be activated by streptokinase showed no significant change of concentration. These observation indicate that plasminogen is not acting as proactivator and that there exists a separate proactivator-activator system of the fibrinolytic mechanism in human serum.

Download Full-text

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.

Download Full-text