Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2001-8-27
pubmed:databankReference
pubmed:abstractText
It is well known that the cytoplasmic streaming of characean cells is readily inhibited by Ca(2+). However, neither the actin-activated MgATPase nor the in vitro motile activity of purified characean myosin were inhibited by Ca(2+). Recently, amino acid sequence of characean myosin was determined in our laboratory and the sequence revealed that characean myosin contains six calmodulin binding sites in the neck region. We also detected calmodulin in quickly prepared characean myosin fraction. It is, therefore, possible that the insensitivity of characean myosin to Ca(2+) is due to the dissociation of some calmodulin molecules from the neck region during the course of protein purification. To determine strictly the Ca(2+) sensitivity of characean myosin, we intentionally used crude preparation of characean myosin to reduce the possibility of calmodulin dissociation and examined the motile activity of characean myosin in vitro in the presence of excess characean calmodulin. We could not observe any drastic inhibition of characean myosin activity by Ca(2+). The results suggest that the brief cessation of cytoplasmic streaming is not caused by the direct inhibition of myosin activity by Ca(2+).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0032-0781
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
828-34
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Effects of Ca(2+) and calmodulin on the motile activity of characean myosin in vitro.
pubmed:affiliation
Department of Biology, Faculty of Science, Chiba University, Yayoi-cho, Inage-ku, Chiba 263-8522 Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't