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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 8
|
| pubmed:dateCreated |
1995-9-14
|
| pubmed:abstractText |
Kinesin is a motor protein that converts chemical energy derived from ATP hydrolysis into mechanical work to transport cellular components along microtubules. We studied the properties of ATP-dependent microtubule-kinesin sliding with two different in vitro assay systems. In one assay system, a kinesin-coated glass microneedle (elastic coefficient, 1-2.5 pN microns -1) was made to slide along an axoneme. Using this system, we obtained the relationship between the force (= load) on the microneedle and the velocity of microneedle-kinesin sliding in the auxotonic condition, in which the load on the microtubule-kinesin contacts increased as sliding progressed. The force-velocity curve was upwardly convex (maximum velocity Vmax, 0.58 +/- 0.15 microns s-1; maximum isometric force P0, 5.0 +/- 1.6 pN) and was similar to that of in vitro actin-myosin sliding in the auxotonic condition, suggesting that the two motor protein systems have fundamental kinetic properties in common. In the other assay system, an axoneme attached to a glass microneedle (elastic coefficient, 4-5 pN microns -1) was made to slide on a kinesin-coated glass surface (Vmax, 0.68 +/- 0.17 microns s-1; P0, 46.1 +/- 18.6 pN). The change in shape of the axoneme indicated an enormous flexibility of randomly oriented kinesin molecules.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0022-0949
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
198
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1809-15
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7636448-Adenosine Triphosphate,
pubmed-meshheading:7636448-Animals,
pubmed-meshheading:7636448-Cattle,
pubmed-meshheading:7636448-Glass,
pubmed-meshheading:7636448-Kinesin,
pubmed-meshheading:7636448-Kinetics,
pubmed-meshheading:7636448-Male,
pubmed-meshheading:7636448-Microtubules,
pubmed-meshheading:7636448-Needles,
pubmed-meshheading:7636448-Sea Urchins,
pubmed-meshheading:7636448-Spermatozoa
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
The mode of ATP-dependent microtubule-kinesin sliding in the auxotonic condition.
|
| pubmed:affiliation |
Department of Physiology, School of Medicine, Teikyo University, Tokyo, Japan.
|
| pubmed:publicationType |
Journal Article
|