Release of a small two-chain form of antithrombin III from a conformationally changed antithrombin III-thrombin complex

Sarah Knoller, Naphtali Savion

Research output: Contribution to journalArticlepeer-review

Abstract

Reaction of antithrombin III (AT) with thrombin results in the formation of stable antithrombin III-thrombin (AT-T) complex with a Mr of 92.5-kDa, accompanied by the appearance of a proteolytically modified form of the inhibitor (ATM). Under these conditions AT-T is also transformed to a smaller complex (AT-TS). This smaller complex (81-kDa), a product of a conformational change at the AT moiety of the AT-T complex, is further transformed to a very small complex (AT-TVS) with a Mr of 71-kDa. Along with this process, AT-TS slowly dissociates to a free enzyme and a small, presumably to-chain product of AT (ATMS) with a Mr of 49-kDa. The newly described component, ATMS, naturally occurs in plasma and serum and accumulates significantly in plasma of patients suffering from cardiovascular disease.

Original languageEnglish
Pages (from-to)203-214
Number of pages12
JournalThrombosis Research
Volume63
Issue number2
DOIs
StatePublished - 15 Jul 1991

Keywords

  • Antithrombin III-Thrombin complex
  • Thrombin modified Antithrombin III

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