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Thromb Haemost 1995; 73(03): 392-397
DOI: 10.1055/s-0038-1653786
Original Articles
Coagulation
Schattauer GmbH Stuttgart

Accelerated Degradation Test of Lyophilized Recombinant Tissue Factor-Liposome Preparations

A M H P van den Besselaar
1   The Haemostasis and Thrombosis Research Centre, Department of Haematology, Leiden University Hospital, Leiden, The Netherlands
,
E Witteveen
1   The Haemostasis and Thrombosis Research Centre, Department of Haematology, Leiden University Hospital, Leiden, The Netherlands
,
Schaefer-van H Mansfeld
1   The Haemostasis and Thrombosis Research Centre, Department of Haematology, Leiden University Hospital, Leiden, The Netherlands
,
J Meeuwisse-Braun
1   The Haemostasis and Thrombosis Research Centre, Department of Haematology, Leiden University Hospital, Leiden, The Netherlands
,
A Strebus
1   The Haemostasis and Thrombosis Research Centre, Department of Haematology, Leiden University Hospital, Leiden, The Netherlands
› Author Affiliations
Further Information

Publication History

Received11 April 1994

Accepted after resubmission 09 November 1994

Publication Date:
09 July 2018 (online)

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Summary

Accelerated degradation experiments were performed to assess the heat stability of lyophilized recombinant tissue factor-liposome preparations from two different manufacturers. When stored at 4° C, these preparations did not show a significant change of the prothrombin time (PT). Two preparations (coded rTF-2 and rTF-a) showed a progressive prolongation of the PT on storage at 30° C, 37° C, and 44° C. The third preparation showed an initial decrease of the PT at 37° C and 44° C followed by a progressive prolongation. Although none of the three preparations was absolutely stable at 30° C, 37° C and 44° C, rTF-2 had the advantage that its PT-ratio (and hence its International Sensitivity Index) did not change under the conditions used in this study. The PT-ratio with a reference material for rabbit brain tissue factor (CRM149S) stored under similar conditions, did not change either.

 

  • References

  • 1 Hetland O, Janson TL, Johnsen B. In vitro effect of phospholipase C from Bacillus Cereus on tissue thromboplastin from different species. Thromb Res 1982; 28: 93-101
    CrossrefPubMedSearch in Google Scholar
  • 2 Nemerson Y. Tissue factor and hemostasis. Blood 1988; 71: 1-8
    PubMedSearch in Google Scholar
  • 3 Ito T, Hiraiwi I, Nishioka J, lino M, Suzuki K. Characterization of functionally important regions of tissue factor by using monoclonal antibodies. J Biochem 1993; 114: 691-696
    CrossrefPubMedSearch in Google Scholar
  • 4 Van den Besselaar AM H P, Van Halem-Visser LP, Loeliger EA, Hermans J. Stability of International Reference Thromboplastins. Br J Haematol 1980; 45: 153-160
    CrossrefPubMedSearch in Google Scholar
  • 5 Van den Besselaar AM H P, Hermans J, Beeser H, Loeliger EA. Long-term stability of international reference preparations for thromboplastins. Br J Haematol 1988; 68: 321-328
    CrossrefPubMedSearch in Google Scholar
  • 6 Kirkwood TB L. Predicting the stability of biological standards and products. Biometrics 1977; 33: 736-742
    CrossrefPubMedSearch in Google Scholar
  • 7 Bangham DR, Biggs R, Brozovic M, Denson KW E. Draft report of a collaborative study of two thromboplastins including the use of common abnormal plasma. Thromb Diathes Haemorrh 1970; Suppl (Suppl. 40) 341-51
    PubMedSearch in Google Scholar
  • 8 Van den Besselaar AM H P, Loeliger EA, Bertina RM. Stability of reference thromboplastins. In: Standardization of Coagulation Assays: An Overview. Triplett DA. ed. College of American Pathologists; Skokie, Illinois; 1982. pp 69-79
    Search in Google Scholar
  • 9 WHO Expert Committee on Biological Standardization. Thirty-third Report. WHO Tech Rep Ser 1983; 687: 81-105
    PubMedSearch in Google Scholar
  • 10 Tripodi A, Arbini A, Chantarangkul V, Mannucci PM. Recombinant tissue factor as substitute for conventional thromboplastin in the prothrombin time test. Thromb Haemost 1992; 67: 42-45
    Thieme ConnectPubMedSearch in Google Scholar
  • 11 Bader R, Mannucci PM, Tripodi A, Hirsh J, Keller F, Solleder EM, Hawkins P, Peng M, Pelzer H, Teijidor LM, Ramirez IF, Kolde HJ. Multicentric evaluation of a new PT reagent based on recombinant human tissue factor and synthetic phospholipids. Thromb Haemost 1994; 71: 292-299
    Thieme ConnectPubMedSearch in Google Scholar
  • 12 Tripodi A, Chantarangkul V, Braga M, Poller L, ten Cate JW, Van den Besselaar AM H P, Mannucci PM. Results of a multicenter study assessing the status of standardization of a recombinant thromboplastin for the control of oral anticoagulant therapy. Thromb Haemost 1994; 72: 261-267
    Thieme ConnectPubMedSearch in Google Scholar
  • 13 Strike PW. Medical Laboratory Statistics. John Wright &; Sons Ltd; Bristol, England: 1981. p 146
    Search in Google Scholar
  • 14 Van den Besselaar AM H P, Meeuwisse-Braun J, Schaefer-Van Mansfeld H. Deterioration of reference material for human thromboplastin. Thromb Haemost 1992; 67: 726
    Thieme ConnectPubMedSearch in Google Scholar
  • 15 Parente RA, Chakraborty UR, Pollick-Andrews B, Riley J, Moore BM. Preparation and characterization of liposome based synthetic thromboplastins. Biophys J 1994; 66: A383
    PubMedSearch in Google Scholar
  • 16 Loeliger EA, Van den Besselaar AM H P, Hermans J, Van der Velde EA. Certification of three reference materials for thromboplastins. BCR CRM no. 147, 148, 149 Commission of the European Communities, BCR information; 1981. pp 25-29
    Search in Google Scholar
  • 17 Paborsky LR, Tate KM, Harris RJ, Yansura DG, Band L, McCray G, Gorman CM, O’Brien DP, Chang JY, Swartz JR, Fung VP, Thomas JN, Vehar GA. Purification of recombinant human tissue factor. Biochemistry 1989; 28: 8072-8077
    CrossrefPubMedSearch in Google Scholar
  • 18 Van den Besselaar AM H P, Bertina RM. Interaction of thromboplastin apo-protein of different tissues with concanavalin A - Evidence for heterogeneous glycosylation of the human apoprotein. Thromb Haemost 1984; 52: 192-195
    Thieme ConnectPubMedSearch in Google Scholar
  • 19 Rudd PM, Joao HC, Coghill E, Fiten P, Saunders MR, Opdenakker G, Dwek RA. Glycoforms modify the dynamic stability and functional activity of an enzyme. Biochemistry 1994; 33: 17-22
    CrossrefPubMedSearch in Google Scholar
  • 20 Greiff D. Protein structure and freeze-drying: the effects of residual moisture and gases. Cryobiology 1971; 8: 145-152
    CrossrefPubMedSearch in Google Scholar
  • 21 Salemink PJ M. Cell and cell constituent freeze-drying: fundamentals and principles. In: Cryopreservation and low temperature biology in blood transfusion. Smit Sibinga CT, Das PC, Meryman HT. eds. Kluwer Academic Publishers; Boston: 1990. pp 25-54
    Search in Google Scholar