Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1988-1-26
pubmed:abstractText
Highly purified microvillar 110 kDa polypeptide-calmodulin (110K-cam) complex was confirmed to have ATPase activities characteristic of a myosin. The effect of F-actin on these activities was investigated. The Mg2+-ATPase is activated about 2-fold by F-actin in a dose-dependent fashion, whereas the K+-EDTA-ATPase is inhibited by greater than 90% by F-actin. These data provide evidence for a functional relationship between the ATPase activity of 110K-cam and its interaction with F-actin. They also extend the similarities between 110K-cam and myosin. The results suggest that higher cells contain in addition to myosin a second class of myosin-like molecules represented by 110K-cam.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
225
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
269-72
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
ATPase activity of the microvillar 110 kDa polypeptide-calmodulin complex is activated in Mg2+ and inhibited in K+-EDTA by F-actin.
pubmed:affiliation
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.