Cytochalasin B-Induced ATPase Activity of Actin: Dependence on Monomer Concentration
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 activit...
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| Veröffentlicht in: | Zeitschrift für Naturforschung C. A journal of biosciences 1981-12, Vol.36 (11), p.1050-1055 |
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| container_end_page | 1055 |
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| container_issue | 11 |
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| container_title | Zeitschrift für Naturforschung C. A journal of biosciences |
| container_volume | 36 |
| creator | Dancker, Peter Kliche, Agnes |
| description | 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. |
| doi_str_mv | 10.1515/znc-1981-11-1224 |
| format | Article |
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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.</description><identifier>ISSN: 0939-5075</identifier><identifier>EISSN: 1865-7125</identifier><identifier>DOI: 10.1515/znc-1981-11-1224</identifier><language>eng</language><publisher>Verlag der Zeitschrift für Naturforschung</publisher><subject>Actin ; Actin Polymerization ; adenosinetriphosphatase ; Cytochalasin B ; polymerization ; rabbits ; skeletal muscle</subject><ispartof>Zeitschrift für Naturforschung C. 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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.</description><subject>Actin</subject><subject>Actin Polymerization</subject><subject>adenosinetriphosphatase</subject><subject>Cytochalasin B</subject><subject>polymerization</subject><subject>rabbits</subject><subject>skeletal muscle</subject><issn>0939-5075</issn><issn>1865-7125</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><recordid>eNp1kL1PwzAQxS0EEqWwM3piM9hJbCdsJXxKRTCU2XLtC6RK7WInoPDX47asSCe9p9N7J90PoXNGLxln_OrHGcKqkhGWJsuKAzRhpeBEsowfogmt8opwKvkxOolxRWkuuOQTtKjH3psP3enYOnxDnpwdDFg8W7zqCHhm-var7Ufsm5131_gWNuAsOAPYO_zsnV9DwLVPC9cH3bfenaKjRncRzv50it7u7xb1I5m_PDzVszkxWVlRArY0ubRFxipY6qUseFNaLqXMrODC2googNCFWJaiMI3NC9okEUZqW1kQ-RRd7O9ugv8cIPZq3UYDXacd-CEqxnMhC7YN0n3QBB9jgEZtQrvWYVSMqi0-lfCpLT7F0iR8qVLvK9-66yFYeA_DmIxa-SG49NX_VbEzjHKa_wKCcXnB</recordid><startdate>19811201</startdate><enddate>19811201</enddate><creator>Dancker, Peter</creator><creator>Kliche, Agnes</creator><general>Verlag der Zeitschrift für Naturforschung</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19811201</creationdate><title>Cytochalasin B-Induced ATPase Activity of Actin: Dependence on Monomer Concentration</title><author>Dancker, Peter ; Kliche, Agnes</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2890-ed8c37d4219ebab745f8d57772d656dd9e0ee6a46b864cfd340fcfd6c7ad9de63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Actin</topic><topic>Actin Polymerization</topic><topic>adenosinetriphosphatase</topic><topic>Cytochalasin B</topic><topic>polymerization</topic><topic>rabbits</topic><topic>skeletal muscle</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dancker, Peter</creatorcontrib><creatorcontrib>Kliche, Agnes</creatorcontrib><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Zeitschrift für Naturforschung C. A journal of biosciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dancker, Peter</au><au>Kliche, Agnes</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochalasin B-Induced ATPase Activity of Actin: Dependence on Monomer Concentration</atitle><jtitle>Zeitschrift für Naturforschung C. A journal of biosciences</jtitle><date>1981-12-01</date><risdate>1981</risdate><volume>36</volume><issue>11</issue><spage>1050</spage><epage>1055</epage><pages>1050-1055</pages><issn>0939-5075</issn><eissn>1865-7125</eissn><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.</abstract><pub>Verlag der Zeitschrift für Naturforschung</pub><doi>10.1515/znc-1981-11-1224</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Zeitschrift für Naturforschung C. A journal of biosciences, 1981-12, Vol.36 (11), p.1050-1055 |
| issn | 0939-5075 1865-7125 |
| language | eng |
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| source | EZB-FREE-00999 freely available EZB journals |
| subjects | Actin Actin Polymerization adenosinetriphosphatase Cytochalasin B polymerization rabbits skeletal muscle |
| title | Cytochalasin B-Induced ATPase Activity of Actin: Dependence on Monomer Concentration |
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