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  Cytochalasin B-induced ATPase activity of actin: dependence on monomer concentration

Dancker, P., & Kliche, A. (1981). Cytochalasin B-induced ATPase activity of actin: dependence on monomer concentration. Zeitschrift für Naturforschung, C: Journal of Biosciences, 36(11-12), 1050-1055. doi:10.1515/znc-1981-11-1224.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0004-F8AF-0 Version Permalink: https://hdl.handle.net/21.11116/0000-0004-F8B0-D
Genre: Journal Article

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ZsNaturforschC_36_1981_1050.pdf (Any fulltext), 6MB
 
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 Creators:
Dancker, Peter1, Author           
Kliche, Agnes1, Author           
Affiliations:
1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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Free keywords: Actin; Actin Polymerization; Cytochalasin B
 Abstract: We simultaneously measured polymerization and ATPase activity of actin induced by cytochalasin B. It was found that under all conditions tested, ATPase activity was proportional to the concentration of actin which was unpolymerized. In addition, it was found that conditions increasing ATPase activity also increase the velocity of polymerization. From this we conclude that CB-induced ATPase activity is a property of the actin monomers and that the “readiness” of the monomers to hydrolyze ATP is correlated with an increased capacity of the monomers to polymerize.

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Language(s): eng - English
 Dates: 1981-06-192014-06-021981-12-01
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1515/znc-1981-11-1224
URI: https://www.ncbi.nlm.nih.gov/pubmed/6459679
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Title: Zeitschrift für Naturforschung, C: Journal of Biosciences
  Abbreviation : Z. Naturforsch., C: J. Biosci.
Source Genre: Journal
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Publ. Info: Berlin : Walter de Gruyter GmbH
Pages: - Volume / Issue: 36 (11-12) Sequence Number: - Start / End Page: 1050 - 1055 Identifier: ISSN: 1865-7125
CoNE: https://pure.mpg.de/cone/journals/resource/954927655916_1