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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-6-6
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pubmed:abstractText |
The presence of alpha-actinin has little influence on polymerizing actin with regards to the lag phase, rate and amplitude. Rising KCl or MgCl2 concentrations parallel an increase in polymerization rate and a decrease in lag phase for both protein species. The observed overall smaller actin fluorescence amplitudes in the presence of alpha-actinin is due to a higher ratio of free G-actin to F-actin at steady state.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1039-9712
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
103-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7735123-Actinin,
pubmed-meshheading:7735123-Actins,
pubmed-meshheading:7735123-Animals,
pubmed-meshheading:7735123-Cations,
pubmed-meshheading:7735123-Deoxyribonuclease I,
pubmed-meshheading:7735123-Fluorescence,
pubmed-meshheading:7735123-Kinetics,
pubmed-meshheading:7735123-Mathematics,
pubmed-meshheading:7735123-Osmolar Concentration,
pubmed-meshheading:7735123-Polymers,
pubmed-meshheading:7735123-Rabbits,
pubmed-meshheading:7735123-Turkey
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pubmed:year |
1995
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pubmed:articleTitle |
The influence of cations and ionic strength on actin polymerization in the presence/absence of alpha-actinin.
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pubmed:affiliation |
Technical University of Munich, Garching, FRG.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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