Air reoxidation and reactivation of reduced thrombin

L. A. Palos, G. Blasko, A. Kosztovics, R. Machovich

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

About 80% of thrombin was inactivated after 50 minutes chemical reduction at 22°C in a reaction mixture containing 0.1 M mercaptoethanol and 2.6 M urea. The reduced protein was spontaneously reoxidated in air at 22°C in 30-60 minutes. The reoxidation of disulphide bonds in thrombin led to partial reactivation of the enzyme. Recovery of thrombin activity after oxidation ranged from 0 to 60% according to the conditions of reoxidation in air. Heparin and copper ion increased the rate of reactivation, whereas in the presence of 10 mM iodoacetamide there was no reactivation.

Original languageEnglish
Pages (from-to)299-303
Number of pages5
JournalActa Physiologica Academiae Scientiarum Hungaricae
Volume51
Issue number3
Publication statusPublished - 1978

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Thrombin
Air
Iodoacetamide
Mercaptoethanol
Disulfides
Heparin
Urea
Copper
Ions
Enzymes
Proteins

ASJC Scopus subject areas

  • Physiology

Cite this

Air reoxidation and reactivation of reduced thrombin. / Palos, L. A.; Blasko, G.; Kosztovics, A.; Machovich, R.

In: Acta Physiologica Academiae Scientiarum Hungaricae, Vol. 51, No. 3, 1978, p. 299-303.

Research output: Contribution to journalArticle

Palos, L. A. ; Blasko, G. ; Kosztovics, A. ; Machovich, R. / Air reoxidation and reactivation of reduced thrombin. In: Acta Physiologica Academiae Scientiarum Hungaricae. 1978 ; Vol. 51, No. 3. pp. 299-303.
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