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Depolymerisation of F-Actin to G-Actin and Its Repolymerisation in the Presence of Analogs of Adenosine Triphosphate

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Mannherz,  Hans Georg
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Brehme,  Helga
Max Planck Institute for Medical Research, Max Planck Society;

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Lamp,  Uli
Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Mannherz, H. G., Brehme, H., & Lamp, U. (1975). Depolymerisation of F-Actin to G-Actin and Its Repolymerisation in the Presence of Analogs of Adenosine Triphosphate. European Journal of Biochemistry, 60(1), 109-116. doi:10.1111/j.1432-1033.1975.tb20981.x.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-FF2F-1
Abstract
A number of ATP analogs were tested for their ability to depolymerize F-actin and interact with it. It was found that those analogues which are hydrolysable are incorporated into the F-actin polymer whereas the non-hydrolysable ones are displaced from the nucleotide binding site during the polymerization process