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• W2077317069 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)." @default.
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• W2077317069 date "1974-06-01" @default.
• W2077317069 modified "2023-10-14" @default.
• W2077317069 title "Cleavage of Actin by Thrombin" @default.
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• W2077317069 doi "https://doi.org/10.1073/pnas.71.6.2208" @default.
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