Altered inactivation of trinitrophenylated thrombin by antithrombin iii in the presence of heparin

R. Machovich, E. Regoeczi, M. W C Hatton

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Modification of bovine α-thrombin by exposure to 2,4,6-trinitrobenzenesulphonic acid and the effects of the modification on the inactivation of the enzyme in the presence of heparin are reported. Transformation of four-five lysine residues resulted in a decrease of the clotting activity of the enzyme by 30-40%, yet its interaction with antithrombin III was not significantly impaired. However, the catalytic effect of heparin on the thrombin-antithrombin III reaction was grossly reduced and the potentiating effects of NaCl and CaC12 on heparin-mediated catalysis was either minimized or no longer apparent.

Original languageEnglish
Pages (from-to)383-391
Number of pages9
JournalThrombosis Research
Volume17
Issue number3-4
DOIs
Publication statusPublished - 1980

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Antithrombins
Thrombin
Heparin
Antithrombin III
Trinitrobenzenesulfonic Acid
Catalysis
Lysine
Enzymes

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine
  • Hematology

Cite this

Altered inactivation of trinitrophenylated thrombin by antithrombin iii in the presence of heparin. / Machovich, R.; Regoeczi, E.; Hatton, M. W C.

In: Thrombosis Research, Vol. 17, No. 3-4, 1980, p. 383-391.

Research output: Contribution to journalArticle

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