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DOI: 10.1055/s-0038-1665299
An Enzyme Linked Immunosorbent Assay for Determination of Tissue Plasminogen Activator Applied to Patients with Thromboembolic Disease
Publication History
Received 13 July 1983
Accepted 11 August 1983
Publication Date:
18 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198303/lookinside/thumbnails/10-1055-s-0038-1665299-1.jpg)
Summary
Utilizing the immunoglobulin fraction from a goat antiserum against human uterine tissue plasminogen activator, an enzyme- linked immunoassay for tissue-type plasminogen activator in human plasma has been developed. With the new method, the concentration of t-PA in normal human acidified plasma is found to be 4.0 ± 1.8 (SD) ng/ml. It increases to 12 ng/ml after a tomiquet test, and to 14 ng/ml after strenous physical exercise. In a group of patients with idiopathic thromboembolic disease, the resting t-PA concentration was 5 ng/ml and the post-occlusion value 16 ng/ml. Furthermore, the patients also exhibited a normal post-occlusion rise in the concentration of plasmin-α2-antiplasmin complex. However, in 37% of the post-occlusion patient plasmas, virtually no increase in t-PA could be detected by a specific activity assay. The results indicate that the reason for a defective post-occlusion fibrinolytic activity in a majority of cases may be the presence of increased concentrations of a fast-acting specific t-PA inhibitor.
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References
- 1 Vermylen JG, Chamone DA F. The role of the fibrinolytic system in thromboembolism. Prog Cardiovasc Dis 1979; 21: 255-266
- 2 Nilsson IM, Krook H, Stemby NH, Söderberg E, Söderström N. Severe thrombotic disease in a young man with bone marrow and skeletal changes and with a high content of an inhibitor in the fibrinolytic system. Acta Med Scand 1961; 169: 323-325
- 3 Isacson S, Nilsson IM. Defective fibrinolysis in blood and vein walls in recurrent “idiopathic” venous thrombosis. Acta Chir Scand 1972; 138: 313-319
- 4 Wallén P, Pohl G, Bergsdorf N, Rånby M, Ny T, Jörnvall H. Purification and structural characterization of a melanom cell plasminogen activator. Eur J Biochem 1983; 132: 681-686
- 5 Wallén P, Rånby M, Bergsdorf N, Kok P. Purification and characterization of tissue plasminogen activator: on the occurrence of two different forms and their enzymatic properties. Progr Fibrinolysis 1981; 5: 16-23
- 6 Rånby M, Norrman B, Wallén P. A sensitive assay for tissue plasminogen activator. Thromb Res 1982; 27: 743-749
- 7 Wiman B, Mellbring G, Rånby M. Plasminogen activator release during venous stasis and exercise as determined by a new specific assay. Clin Chim Acta 1982; 127: 279-288
- 8 Wiman B, Jacobsson L, Andersson M, Mellbring G. Determination of plasmin-α2-antiplasmin complex in plasma samples by means of a radioimmunoassay. Scand J Clin Lab Invest 1983; 43: 27-33
- 9 Jeppsson JO, Laurell CB, Franzén B. Agarose Gel Electrophoresis. Clin Chem 1979; 25: 629-638
- 10 Laurell CB. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 1966; 15: 45-52
- 11 Engvall E. Enzyme immunoassay ELISA and EMIT. Methods Enzymol 1980; 70 A 419-439
- 12 Rijken DO, Juhan-Vague I, de Cock F, Collen D. Measurement of human tissue-type plasminogen activator by a two-site immunoradiometric assay. J Lab Clin Med 1983; 101: 274-284
- 13 Korninger C, Collen D. Neutralization of human extrinsic (tissue- type) plasminogen activator in human plasma: no evidence for a specific inhibitor. Thromb Haemostas 1981; 46: 662-665
- 14 Chmielewska J, Rånby M, Wiman B. Evidence for a rapid inhibitor to tissue plasminogen activator. Thromb Res. 1983 (in press)