Cleavage of actin by thrombin

L. Muszbek, K. Laki

Research output: Contribution to journalArticle

33 Citations (Scopus)

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).

Original languageEnglish
Pages (from-to)2208-2211
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume71
Issue number6
Publication statusPublished - 1974

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Thrombin
Actins
Molecular Weight
Divalent Cations
Edetic Acid
Sodium Dodecyl Sulfate
Sucrose
Digestion
Nucleotides

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Cleavage of actin by thrombin. / Muszbek, L.; Laki, K.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 71, No. 6, 1974, p. 2208-2211.

Research output: Contribution to journalArticle

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