PubMed Health⌕ Search

Biomedical subjects

F Duckert

Publications and source records attributed to F Duckert.

At least 73 records · Page 4Linked to original sources
PubMed1982

Sequential treatment of arterial occlusions with porcine plasmin and low dose streptokinase.

Sequential treatment of arterial occlusions of the leg with porcine plasmin and low dose streptokinase results in a strong systemic proteolysis as already seen in deep leg vein thrombosis. In 31 of 45 patients the blood flow through major arterial segments could be restored. Thrombolytic success is possible within the first two treatment days but for the majority of the cases fibrinolytic therapy for 3-6 days is needed. On the average treatment was 1 day shorter than in DVT cases. No statistical relationship between local thrombolysis and systemic proteolysis was detected. The thrombolytic efficacy of this regimen compares favourably with earlier experience on fibrinolytic therapy in arterial occlusions.

Adult↗
PubMed1982

Sequential treatment of deep leg vein thrombosis with porcine plasmin and low dose streptokinase.

Sequential treatment of deep leg vein thrombosis with porcine plasmin and low dose streptokinase (10,000-20,000 U/h) produces strong systemic fibrinolysis as demonstrated by the sustained decrease of euglobulin lysis time, of thromboplastin time values in percent, fibrinogen and factor V levels. There is a statistically significant negative correlation between thrombolytic results and euglobulin lysis time. Treatment period below 3 days are unlikely to give satisfactory results. Occluded vein segments with an apparent median age of 4 days including thrombi older than 10 days (20% of cases) are cleared with an average chance of 50%. Complete dissolution of all thrombi proximal to the crural veins has been demonstrated in 47/114 = 41.2%, some thrombolytic effects in 31/114 = 27.2% and treatment failure in 36/114 = 31.6%. The data favour laboratory monitoring of thrombolytic therapy.

Adult↗
PubMed1982

Side effects of thrombolytic treatment with porcine plasmin and low dose streptokinase.

In the sequential thrombolytic therapy with porcine plasmin and low dose streptokinase side effects are mainly due to bleeding, intolerance reactions are less important. Treatment had to be prematurely stopped in 42 (37%) of 114 DVT cases because of severe bleeding and in 12 (10%) due to intolerance reactions. The corresponding figures for the 45 cases with arterial occlusions are 15 (33%) and 2 (4%) respectively. The intensity of systemic proteolysis as represented by the thromboplastin time is significantly correlated with haemorrhagic manifestations. Macrohematuria and bleeding from puncture sites are the most frequent haemorrhagic complications followed by spontaneous bleeding into skin and muscles. Non-fatal intracranial bleeding occurred in 1 DVT case (0.9%) and in 2 patients with arterial occlusions (4.4%). The benefit of this potent thrombolytic regimen would greatly improve if a strong reduction of premature treatment stop could be achieved.

Animals↗
PubMed1981

Rabbit antibodies against the procoagulant activity (VIII:C) of human factor VIII. Some theoretical and practical considerations on the human factor VIII molecule using heterologous antibodies.

The procoagulant activity VIII:C was separated from factor VIII antigen (VIIIR:Ag) by gel filtration in the presence of 0.25 mol/l calcium chloride. Antibodies (anti-VIII:C) were obtained by immunization of rabbits with VIII:C. The last step of the purification procedure of antibodies consists of an adsorption on VIIIR:Ag-Sepharose 2 BCL as immunoadsorbent to remove contaminating traces of antibodies against VIIIR:Ag. The anti-VIII:C titer remains unchanged during this adsorption (29 Bethesda units per mg). In solution, anti-VIII:C neutralizes factor VIII activity (in plasma, cryoprecipitate or in purified form) and the fragment VIII:C without reacting with VIIIR:Ag. Once immobilized on a solid matrix, i.e. 2% agarose, it loses over 95% of its inhibitory capacity. The immobilized anti-VIIIR:Ag binds stoichiometrically the antigen and the activity of plasma factor VIII. These results together suggest that factor VIII is composed of 2 different entities, but undissociated under physiological conditions. Immunophysical analyses as a function of pH and temperature of anti-VIII:C and its complex with factor VIII show properties similar to those of homologous antibodies. The antigen determinants of VIII:C (VIII:CAg) are destroyed at low pHs or high temperatures, and VIII:C can no more form a complex with anti-VIII:C. Purified anti-VIII:C is also used in a two-stage assay to detect VIII:CAg or cross-reacting material in some severe haemophiliacs.

Animals↗
PubMed1980

Monitoring of oral anticoagulation by an amidolytic factor X assay. A long-term study in 42 patients.

The validity of the amidolytic Factor X assay for the control of long term oral anticoagulation (OA) was investigated in 42 patients randomized into 2 groups; PT group (anticoagulant dosage according to PT) and F.X group (anticoagulant dosage based on F.X). An independent expert's dosage according to F.X served for analysis in the former group. In the F.X group the F.X based dosage was considered valid only when not differing by more than 15% from the expert's PT based dosage. Confirming the good correlation between PT and F.X the study further demonstrates that the changes from one control to the next one, delta PT and delta F.X, too, are significantly correlated (r = 0.58, p less than 0.001, n = 217). In over one third of the periods the dosage proposals based on PT and F.X were identical and differed by more than 15% in only 12/217 instances. Our results justify a large trial on the control of OA by the amidolytic F.X assay.

4-Hydroxycoumarins↗
PubMed1980

Reactivity of a hereditary abnormal antithrombin III fraction in the inhibition of thrombin and factor Xa.

Two different AT-III fractions were purified from the plasma of a patient with recurrent superficial thrombophlebitis. The abnormal AT-III fraction (A-AT) was compared to the normal AT-III fraction (N-AT) in the inhibition of thrombin and factor Xa. Without heparin, both inactivate proteases in a similar manner and at the same rate. However, at low heparin concentration the thrombin inhibition proceeds more slowly with A-AT than with N-AT. At high heparin concentration the difference between A-AT and N-AT becomes very small. The inhibition of factor Xa follows a similar pattern. It is suggested that the heparin binding site of A-AT differs from that of N-AT resulting in a decreased heparin cofactor activity.

Antithrombin III↗
PubMed1980

Different assessment of plasmin with different substrates. In vitro alteration of plasmin, influence of epsilon-aminocaproic acid and tranexamic acid upon its activity.

The alteration of human and porcine plasmin and the influence of EACA and AMCHA on their activity were investigated. Solutions of both plasmins undergo storage induced alteration, which is best recorded by Chromozym PL, whereas the other chromogenic substrates, S-2251 and S-2302, and casein are less sensitive, and the fibrin plate inadequate. Plasmin amidolytic and fibrinolytic activity is maximally enhanced at 7.6 x 10(-3) M EACA and 6.4 x 10(-4) M AMCHA, and decay through storage is reversed. The caseinolytic activity seems slightly inhibited at the same EACA and AMCHA concentrations. Our results show: 1. The quotient: plasmin activity towards Chromozym PL/Activity towards S-2251 is a useful indicator of "plasmin quality". The quotient decreases markedly upon storage of plasmin solutions. 2. Plasmin stability is improved in the presence of AMCHA. 3. It is valueless to add EACA or AMCHA to inhibit plasmin in amidolytic assays since the chosen concentration enhances the amidolytic activity of already formed plasmin.

Aminocaproates↗
PubMed1980

Monitoring of heparin treatment. Comparison of thrombin time, activated partial thromboplastin time, and plasma heparin concentration, and analysis of the behavior of antithrombin III.

Three laboratory methods for monitoring heparin treatment have been compared using 63 plasma samples: the thrombin time, the activated partial thromboplastin time, and the measurement of the heparin concentration using a chromogenic substrate. A good correlation was found between the methods. However, the intensity of anticoagulation was identical in only 27 of the 63 samples (43%) when the thrombin time and the activated partial thromboplastin time were compared. Fully discordant results were recorded for four samples (6%). The thrombin time was found to be more closely related to the plasma heparin concentration than was the activated partial thromboplastin time. Both antithrombin-III activity and immunologic levels were lower in the group with strong heparinization. It is suggested that the thrombin time is a good and safe method for monitoring heparin treatment.

Antithrombin III↗
PubMed1979

[Control of oral anticoagulation: comparison between Quick and colorimetric factor X determination in 107 patients].

Since monitoring of oral anticoagulation (OA) by prothrombin time (PT) is a source of standardization difficulties, the authors have tested another approach. 107 patients under long term OA were monitored by both PT and a colorimetric factor X assay (in vitro activation of factor X with RVV and assessment of amidolytic activity towards S-2222). The PT values were between 10 and 34% (therapeutic range 15--25%), and factor X levels were between 10 and 44% (therapeutic range 16--24%). The correlation between the two methods was highly significant (r = 0.65, p less than 0.001). In 68% of the patients the two tests gave the same information (55 subjects were adequately, 16 insufficiently and 2 over-anticoagulated). For a slightly broader therapeutic range (PT 15--30%, corresponding to 16--28% factor X) concordant information was obtained in 82% of the patients. During stable OA, PT and factor X assay gave very similar information. An advantage of the latter method is the possibility of automation, while a disadvantage is its insensitivity to factor VII.

Administration, Oral↗
PubMed1979

[Dissociation of human factor VIII and recombination of the fragments VIII-C and VIII-AG].

Human factor VIII has been dissociated into fragment VIII-C and fragment VIII-AG in the presence of calcium chloride (0.25 M). After removing the calcium, recombination of the molecule is obtained. Fragment VIII-C can be activated by thrombin in a similar manner to the coagulant activity of whole factor VIII. This activation is calcium-dependent. In rabbits immunized against purified F VIII, VIII-C and VIII-AG specific antisera against these three entities were obtained.

Blood Coagulation Tests↗
PubMed1979

[Basle family study. Organization and 1st results].

The organisation of the Basle Family Study and preliminary results outlining the data analysis are presented. The study investigates in 500 families the familial influence on risk factors for cardiovascular diseases. In addition the distribution of hemostatic variables is studied. Analysis of the data according to age, sex and intrafamilial relations in 211 families demonstrate the influence of the mother on the development of the life style of the children.

Adolescent↗