Linked Life Data

8947842

Source:http://linkedlifedata.com/resource/pubmed/id/8947842

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-3-17
pubmed:abstractText
We have examined the temperature-dependence of sliding velocity of fluorescent F-actin on myosins isolated from 10 degrees C- and 30 degrees C-acclimated carp. Activation energies for the sliding of F-actin were 63 and 111 kJ/mol for the 10 degrees C- and 30 degrees C-acclimated carp myosins, respectively. Arrhenius plots of the sliding velocity from 10 degrees C- and 30 degrees C-acclimated carp myosin were shown to intersect at high temperature (about 30 degrees C). The thermostability estimated by measuring the Ca(2-)-ATPase activity was less for myosin from 10 degrees C- than 30 degrees C-acclimated carp. We suggest that a less thermostable structure in cold-acclimated carp myosin results in a reduced activation energy for the contractile process, which allows the F-actin to slide fast even at low temperatures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
120
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
788-91
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Lower activation energy for sliding of F-actin on a less thermostable isoform of carp myosin.
pubmed:affiliation
Department of Physiology, School of Medicine, Teikyo University, Tokyo. chaen@med.teikyo-u.ac.jp
pubmed:publicationType
Journal Article, In Vitro