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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1989-11-14
|
| pubmed:abstractText |
The sliding distance of an actin filament induced by a myosin head during one ATP hydrolysis cycle was determined by measuring minimum length of actin filaments moving on myosin-coated glass surface as fast as long ones and the ATPase rate during sliding. The results indicate that the sliding distance is greater than 100nm, suggesting that the mechanical reaction can occur many times during one chemical (ATP hydrolysis) cycle.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0361-7742
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
315
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
27-36
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:2529564-Actins,
pubmed-meshheading:2529564-Actomyosin,
pubmed-meshheading:2529564-Adenosine Triphosphatases,
pubmed-meshheading:2529564-Energy Metabolism,
pubmed-meshheading:2529564-Microscopy, Electron,
pubmed-meshheading:2529564-Microscopy, Fluorescence,
pubmed-meshheading:2529564-Models, Chemical,
pubmed-meshheading:2529564-Muscles,
pubmed-meshheading:2529564-Myosins,
pubmed-meshheading:2529564-Video Recording
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
The elementary process in the actomyosin energy transduction system.
|
| pubmed:affiliation |
Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
|
| pubmed:publicationType |
Journal Article
|