Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
25
|
| pubmed:dateCreated |
1990-10-9
|
| pubmed:abstractText |
A pair of 10-kDa peptides, designated CB-a and CB-b, was isolated by calmodulin-Sepharose chromatography from a total CNBr digest of turkey gizzard caldesmon. CB-a encompasses the COOH-terminal segment of residues 659-756, according to the sequence of adult chicken gizzard caldesmon (Bryan, J., Imai, M., Lee, R., Moore, P., Cook, R.G., and Lin, W.G. (1989) J. Biol. Chem. 264, 13873-13879), whereas CB-b comprises the same structure but was a few amino acids shorter at its COOH terminus. Both peptides cosedimented with F-actin, and their binding was increased by smooth muscle tropomyosin. The Kd values were 1.3 and 0.5 microM, in the absence and presence of tropomyosin, respectively, with a maximum binding capacity of 6.9 actins/mol of peptides. The CB-a/CB-b fragments inhibited, in a tropomyosin-sensitive and Ca2(+)-calmodulin-dependent manner, the skeletal actomyosin subfragment 1 ATPase activity to a level close but not identical to that observed for the parent caldesmon. Ca2(+)-calmodulin was selectively cross-linked to either caldesmon or the CNBr peptides with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide producing 1:1 covalent complexes that were retained neither by phenyl-Sepharose nor by immobilized calmodulin. Moreover, the cross-linked caldesmon bound weakly to F-actin and did not inhibit the actomyosin subfragment 1 ATPase in the absence of Ca2+. The results suggest that the CB-a/CB-b peptide region contains major regulatory determinants of caldesmon.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Tropomyosin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
265
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
15231-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2394719-Actins,
pubmed-meshheading:2394719-Animals,
pubmed-meshheading:2394719-Binding, Competitive,
pubmed-meshheading:2394719-Binding Sites,
pubmed-meshheading:2394719-Calmodulin,
pubmed-meshheading:2394719-Calmodulin-Binding Proteins,
pubmed-meshheading:2394719-Chromatography, Affinity,
pubmed-meshheading:2394719-Cyanogen Bromide,
pubmed-meshheading:2394719-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2394719-Gizzard,
pubmed-meshheading:2394719-Kinetics,
pubmed-meshheading:2394719-Molecular Weight,
pubmed-meshheading:2394719-Muscle, Smooth,
pubmed-meshheading:2394719-Muscles,
pubmed-meshheading:2394719-Peptide Fragments,
pubmed-meshheading:2394719-Rabbits,
pubmed-meshheading:2394719-Tropomyosin,
pubmed-meshheading:2394719-Turkeys
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Characterization of the carboxyl-terminal 10-kDa cyanogen bromide fragment of caldesmon as an actin-calmodulin-binding region.
|
| pubmed:affiliation |
Institut, National de la Santé et de la Recherche Médicale U. 249, Université de Montpellier I, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|