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Biomedical subjects

S Lopaciuk

Publications and source records attributed to S Lopaciuk.

99 records · Page 6Linked to original sources
PubMedDate not supplied

[Preparation and clinical use of a new factor IX concentrate].

Factor IX concentrate was obtained using DEAE-Sephadex A-50 as an adsorbent. The yield of factor IX in vitro averaged 81%. Each bottle of the concentrate contained 288-512 u. of factor II, 96--360 u. of factor VII, 440--660 u. of factor IX and 256--680 u. of factor X. The results of studies showed trace amounts of factor Xa in the final product, in the range of 0.01--0.04 u/ml. The concentrate was found to be free of thrombin. In the years 1976--1977 the new concentrate was administered 48 times to 10 patients with severe haemophilia B. The in vivo recovery of factor IX was 27--65%. Clinical results of treatment were satisfactory in all patients. No significant changes were observed in platelet count, fibrinogen level and the concentration of fibrinogen degradation products after infusion of the concentrate. The ethanol gelation test was negative in all cases.

Adolescent↗
PubMedDate not supplied

[Factor VIII complex activities in acute leukemia].

Factor VIII procoagulant activity (VIII:C), factor VIII related antigen (VIIIR:AG) and von Willebrand factor activity (ristocetin cofactor, VIII:WF) were estimated in plasma from 37 patients with acute leukaemia. Of 25 patients in the active state of the disease, before or during cytostatic treatment, 19 (76%) showed abnormally high VIIIR:AG levels, between 240 and 780 U/100 ml. Fifteen of them also had elevated VIII:C and VIII:WF (184--480 U/100 ml and 182--360 U/100 ml respectively). The ratio of VIIIR:AG to VIII:C in this group of patients ranged from 0.53 to 4.39 with a mean of 1.35 +/- 0.8. Of 12 patients in partial or complete remission, only 3 (25%) had elevated VIIIR:AG. Four other patients showed high levels of VIII:C and normal values for VIIIR:AG and VIII:WF. The ratio of VIIIR:AG to VIII:C in the patients during remission ranged from 0.46 to 2.86 with a mean of 0.98 +/- 0.7. No relationship was apparent between the factor VIII-related activities and cytochemical type of leukaemia or leucocyte count in peripheral blood. Crossed antigen-antibody electrophoresis of factor VIII protein which was performed in 5 patients with high levels of VIIIR:AG turned up to be completely normal. In the vast majority of patients, plasma fibrinogen and serum fibrinogen degradation products were within the normal range.

Adolescent↗
PubMedDate not supplied

[Polish hydroxyethyl starch preparation: a clinical study].

The 6% solution of hydroxyethyl starch (MS = 0.47-0.7, Mw = 120,000-220,000) prepared at the Department of Biochemistry, Institute of Haematology in Warsaw was administered in infusions to a group of surgical patients. It was found that the preparation complied with the conditions and requirements for plasma-replacing agents. In none of the treated patients any side effects were observed. Further investigations will be continued infusing greater volumes of HES to patients with hypovolaemia of different origin.

Adult↗
PubMedDate not supplied

Prevalence of heparin cofactor II deficiency in patients with a history of venous thrombosis.

Heparin cofactor II (HC II) is a plasma glycoprotein which inhibits thrombin but not factor Xa and which requires heparin or other glycosaminoglycans for its activation. Although several pedigrees have been reported in which 50% decreases in plasma HC II were associated with venous or arterial thrombosis, the role of HC II deficiency in inherited thrombophilia remains unproved. The present study was performed to determine the prevalence of HC II deficiency among patients with a history of venous thrombosis. HC II antigen was measured by electroimmunoassay in 122 unrelated patients with first episode of deep vein thrombosis developed before the age of 45 and in 114 healthy volunteers. Of the controls, 1 had a low HC II concentration (37%), while in the remaining 113, levels ranged from 65 to 180% with the mean value of 98.6 +/- 20.6%. In thrombosis patients, the mean HC concentration was 99.9 +/- 28.0%: individual values ranged from 52 to 180%. Seven patients (5.7%) exhibited values beneath the lower limit of the normal range (65%). These results indicate that HC II deficiency is more prevalent among patients with venous thromboembolism than in healthy subjects.

Adult↗
PubMedDate not supplied

[Detection of Hemophilia A carrier state].

Factor VIII biological activity and factor-VIII-related antigen were measured in the plasma of 78 definite, probable or potential carriers of haemophilia A and in a control group of 74 normal women. Low values of factor VIII activity could be detected in 11 of 24 definite carriers, in 11 of 26 probable carriers and, in 10 of 28 potential carriers. On the other hand, the ratio of factor VIII activity to factor-VIII-related antigen was significantly lowered in 79 percent of definite carriers, in 50 percent of probable carriers and, in 21 percent of potential carriers. These studies indicate that determinations of both factor VIII activity and antigen is more reliable procedure in the detection of the carrier state for haemophilia A than determinations of factor VIII activity alone.

Adolescent↗
PubMedDate not supplied

[Isolation and some properties of factor VIII (antihemophilic factor)].

A method for isolation of factor VIII from cryoprecipitate fraction of human plasma has been elaborated. The isolation procedure involves precipitation with dextran, removal of fibrinogen by means of defibrase, precipitation with ammonium sulfate, polyethylene glycol fractionation, and Sepharose 6B gel filtration step. Factor VIII has been purified 7000- to 13,000 -- fold.. The preparation is homogenous by ultracentrifugal examination and it has an S20,w value of 19.4. It also shows a single precipitin line when subjected to immunoelectrophoresis employing rabbit antibodies against factor VIII. The preparation did not enter a 7.5% polyacrylamide gel containing sodium dodecyl sulfate even in the presence of 8 M urea. After reduction of the protein with 2-mercaptoethanol, subunits were formed which migrated as one band in polyacrylamide gel electrophoresis.

Antibodies↗