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. 1974 Jun;71(6):2208–2211. doi: 10.1073/pnas.71.6.2208

Cleavage of Actin by Thrombin

L Muszbek 1,*, K Laki 1
PMCID: PMC388420  PMID: 4210209

Abstract

Under certain conditions actin can be split by thrombin. Actin prepared in the presence of excess Ca++ was found to be resistant to thrombin. However, if actin was purified without added Ca++, both G- and F- actin underwent thrombic digestion, although a considerable proportion of actin molecules remained intact. Similar results were obtained with actin (in 50% sucrose) devoid of nucleotide and divalent cations but retaining its native characteristic. The removal of tightly bound Ca++ from actin by EDTA accelerated the thrombic splitting and made the complete fragmentation of G-actin possible. Thrombin first cleaves actin into two pieces and subsequently one of them, fragment K (molecular weight 37,000 on sodium dodecyl sulfate-polyacrylamide gel), splits further, resulting in fragments L (molecular weight 27,000) and M (molecular weight about 10,000).

Keywords: clot retraction, contractile proteins, ATP-binding

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Selected References

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