Download PDF
Thromb Haemost 1983; 50(02): 563-566
DOI: 10.1055/s-0038-1665256
Original Article
Schattauer GmbH Stuttgart

Determination of Factor XIII Activity and of Factor XIII Inhibitors Using an Ammonium-Sensitive Electrode

P Hellstern
The Department of Clinical Hemostaseology and Transfusion Medicine, University of the Saarland, Homburg/Saar, F.R.G.
,
K Schilz
The Department of Clinical Hemostaseology and Transfusion Medicine, University of the Saarland, Homburg/Saar, F.R.G.
,
G von Blohn
The Department of Clinical Hemostaseology and Transfusion Medicine, University of the Saarland, Homburg/Saar, F.R.G.
,
E Wenzel
The Department of Clinical Hemostaseology and Transfusion Medicine, University of the Saarland, Homburg/Saar, F.R.G.
› Author Affiliations
Further Information

Publication History

Received 18 February 1983

Accepted 08 June 1983

Publication Date:
18 July 2018 (online)

Also available at
  PDF Download  Permissions and Reprints

Summary

An assay for rapid factor XIII activity measurement has been developed based on the determination of the ammonium released during fibrin stabilization. Factor XIII was activated by thrombin and calcium. Ammonium was measured by an ammonium-sensitive electrode. It was demonstrated that the assay procedure yields accurate and precise results and that factor XIII-catalyzed fibrin stabilization can be measured kinetically. The amount of ammonium released during the first 90 min of fibrin stabilization was found to be 7.8 ± 0.5 moles per mole fibrinogen, which is in agreement with the findings of other authors. In 15 normal subjects and in 15 patients suffering from diseases with suspected factor XIII deficiency there was a satisfactory correlation between the results obtained by the “ammonium-release-method”, Bohn’s method, and the immunological assay (r1 = 0.65; r2= 0.70; p<0.01). In 3 of 5 patients with paraproteinemias the values of factor XIII activity determined by the ammonium-release method were markedly lower than those estimated by the other methods. It could be shown that inhibitor mechanisms were responsible for these discrepancies.

Keywords

Factor XIII activity - Inhibitors of fibrin stabilization - Ammonium release - Ammonium-sensitive electrode
 

  • References

  • 1 Bohn H. Immunologische Untersuchungen über Faktor XIII und das FSF-bindende Globulin. Blut 1974; 28: 81-89
    CrossrefPubMedSearch in Google Scholar
  • 2 Bohn H, Haupt H. Eine quantitative Bestimmung von Faktor XIII mit Anti-Faktor-XIII-Serum. Thrombos Diathes Haemorrh 1968; 19: 309-315
    PubMedSearch in Google Scholar
  • 3 Sigg PE, Duckert F. Ein neuer Test zur Bestimmung des fibrinstabilisierenden Faktors (FSF). Schweiz Med Wochenschr 1963; 93: 1455-1456
    PubMedSearch in Google Scholar
  • 4 Lorand L, Rule NG, Ong HH, Furlanetto R, Jagobsen A, Downey J, Oner N, Bruner-Lorand J. Amine specifity in transpeptidation. Inhibition of fibrin cross-linking Biochemistry 1968; 7: 1214-1223
    CrossrefPubMedSearch in Google Scholar
  • 5 Lorand L, Urayama T, de KiewietJ, Nossel HL. Diagnostic and genetic studies on fibrin-stabilizing factor with a new assay based on amine incorporation. J Clin Invest 1969; 48: 1054-1064
    CrossrefPubMedSearch in Google Scholar
  • 6 Lorand L, Campbell-Wilkes LK, Cooperstein L. A filter paper assay for transamidating enzymes using radioactive amine substrates. Anal Biochem 1972; 50: 623-631
    CrossrefPubMedSearch in Google Scholar
  • 7 Lorand L, Chenoweth D, Gray A. Titration of the acceptor crosslinking sites in fibrin. Ann NY Acad Sei 1972; 202: 155-171
    CrossrefPubMedSearch in Google Scholar
  • 8 Loewy AG. Wirkungsmechanismus des Faktor XIII. Thrombos Diathes Haemorrh 1968; 28: 1-12
    PubMedSearch in Google Scholar
  • 9 Wenzel E, Christ G. Untersuchungen über die Entstehung von Ammoniak im Zitratplasma nach Rekalzifizierung. Thrombos Diathes Haemorrh 1969; 22: 575-576
    PubMedSearch in Google Scholar
  • 10 Clauss A. Gerinnungsphysiologische Schnellmethode zur Bestimmung des Fibrinogens. Acta Haematol 1957; 17: 237-246
    CrossrefPubMedSearch in Google Scholar
  • 11 Guide to the use of ion selective electrodes. Liquid membrane IS 5660 series. Philips Industries Eindhoven. 1973 1. 1-48
    PubMedSearch in Google Scholar
  • 12 Beck EA. Congenital disorders of fibrin formation and stabilization. In Haemostasis and Thrombosis. Colman RW, Hirsh J, Marder VJ, Salzman EW. (Eds) J. B. Lippincott Company; hiladelphia-Toronto: 1982. pp 185-209
    Search in Google Scholar
  • 13 Miloszweski K, Wall WD, Losowsky MS. Absence of plasma transamidase activity in congenital deficiency of fibrin stabilizing factor (factor XIII). Br J Haematol 1969; 17: 159-162
    CrossrefPubMedSearch in Google Scholar
  • 14 Dvilansky A, Britten AF, Loewy AG. Factor XIII assay by an isotope method. II Heparin inhibition of factor XIII activation. Thrombos Diathes Haemorrh 1970; 24: 256-264
    PubMedSearch in Google Scholar
  • 15 Carlebjürk G. A precise routine method for determination of f XIII activity in plasma. Thromb Res 1981; 21: 507-511
    CrossrefPubMedSearch in Google Scholar
  • 16 Rasche H. Blutgerinnungsfaktor XIII und Fibrinstabilisierung. Wochenschr Klin 1975; 53: 1137-1145
    PubMedSearch in Google Scholar
  • 17 Schwartz ML, Pizzo SV, Hill RL, McKee PA. The effect of fibrin- stabilizing factor on the subunit structure of human fibrin. J Clin Invest 1971; 50: 1506-1513
    CrossrefPubMedSearch in Google Scholar
  • 18 Britten AF. Congenital deficiency of factor XIII (fibrin stabilizing factor): Report of a case and review of the literature. Am J Med 1967; 43: 751-761
    CrossrefPubMedSearch in Google Scholar
  • 19 Losowsky MS, Hall R. Estimation of plasma fibrin stabilizing factor in families showing congenital deficiencies. Clin Sei 1966; 30: 171-178
    PubMedSearch in Google Scholar
  • 20 Wall WD, Losowsky MS. Abnormalities of fibrin stabilization in liver disease and kidney disease: A comparison of two different methods. Clin Sri 1969; 37: 837-846
    PubMedSearch in Google Scholar
  • 21 Folk JE, Finlayson JS. The ∈-(γ-Glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv Protein Chem 1977; 31: 1-133
    PubMedSearch in Google Scholar