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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4 Suppl
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pubmed:dateCreated |
1995-7-27
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pubmed:abstractText |
We have measured the ATPase activity of squid optic lobe kinesin bound to polystyrene beads in the presence of microtubules. We find that there is a substantial increase (> 10-fold) in the microtubule-activated ATPase activity for bead-bound kinesin over free kinesin. We tentatively attribute such cargo-activated ATPase activity to the presence of a self-inhibited form of kinesin in solution, which becomes activated when bound to a bead in the presence of alpha-casein. Further experiments are underway to unravel this phenomenon and, in addition, to associate the traveling distance of beads with the observed ATPase rate to determine the average number of ATP consumed per kinesin-bead per micron of travel along microtubule.
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pubmed:commentsCorrections |
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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 |
Apr
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
68
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
283S-284S; discussion 285S
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7787091-Adenosine Triphosphatases,
pubmed-meshheading:7787091-Adenosine Triphosphate,
pubmed-meshheading:7787091-Animals,
pubmed-meshheading:7787091-Biophysical Phenomena,
pubmed-meshheading:7787091-Biophysics,
pubmed-meshheading:7787091-Decapodiformes,
pubmed-meshheading:7787091-Hydrolysis,
pubmed-meshheading:7787091-Kinesin,
pubmed-meshheading:7787091-Kinetics,
pubmed-meshheading:7787091-Microtubules,
pubmed-meshheading:7787091-Movement,
pubmed-meshheading:7787091-Optic Lobe, Nonmammalian
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pubmed:year |
1995
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pubmed:articleTitle |
Cargo-activated ATPase activity of kinesin.
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pubmed:affiliation |
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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