Cleavage of Actin by Thrombin
- 1 June 1974
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 71 (6), 2208-2211
- https://doi.org/10.1073/pnas.71.6.2208
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
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