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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1988-1-7
|
| pubmed:abstractText |
The actin-binding property of the myosin head 20 K (K = 10(3) Mr) fragment has been examined by a structural assay. A new fragment is produced by digestion of scallop myosin synthetic filaments with a lysine-specific protease. This fragment consists of the rod together with two "nubs" corresponding to the 20 K fragment, which retain both the regulatory and essential light chains. Myosin filaments, digested for different lengths of time, were mixed with F-actin and visualized by electron microscopy after negative staining. When the head is cleaved, but the head fragments remain associated, the filaments bind actin in an ATP-sensitive manner. Filaments made primarily of the nub-containing fragments, however, bind actin very poorly. In addition, electron microscopic characterization of actin-binding by the isolated tryptic 20 K fragment from chicken myosin indicates that binding of this fragment to actin is probably non-specific. These results suggest that interactions between the 20 K region and the other peptides in the head are essential for actin-binding.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0022-2836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
196
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
955-60
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading | |
| pubmed:year |
1987
|
| pubmed:articleTitle |
Myosin binding to actin. Structural analysis using myosin fragments.
|
| pubmed:affiliation |
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|