| pubmed-article:3709514 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C1267092 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C0001291 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C0006746 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C0392752 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C0443220 | lld:lifeskim |
| pubmed-article:3709514 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:3709514 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3709514 | pubmed:dateCreated | 1986-6-30 | lld:pubmed |
| pubmed-article:3709514 | pubmed:abstractText | A rapid purification procedure has been developed for the isolation of caldesmon from hog stomach smooth muscle utilizing a KI extract of washed myofibrils as source material. On SDS-PAGE this mammalian caldesmon showed a closely-spaced doublet around 155 kd. By low-angle rotary shadowing caldesmon was shown to be an elongated, highly flexible molecule which tends to form end-to-end dimers that are structurally very similar to filamin. When added to F-actin solutions caldesmon increased the high-shear viscosity considerably, but by an extent that depended on sample preparation. The effect was shown to be due to caldesmon and not to a trace contaminant by its full reversibility after addition of a monospecific caldesmon antibody. Recent investigations have shown that in smooth muscle two structurally distinct domains can be distinguished: an actomyosin domain and an actin-intermediate filament domain. Immunocytochemistry of ultrathin sections of smooth muscle at the light and electron microscope level revealed that caldesmon is present in the actomyosin domain. Caldesmon is thus a potential regulator of the actomyosin system in smooth muscle. | lld:pubmed |
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| pubmed-article:3709514 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3709514 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3709514 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3709514 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:3709514 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:3709514 | pubmed:author | pubmed-author:SmallJ VJV | lld:pubmed |
| pubmed-article:3709514 | pubmed:author | pubmed-author:De MeyJJ | lld:pubmed |
| pubmed-article:3709514 | pubmed:author | pubmed-author:CrossR ARA | lld:pubmed |
| pubmed-article:3709514 | pubmed:author | pubmed-author:FürstD ODO | lld:pubmed |
| pubmed-article:3709514 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3709514 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:3709514 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3709514 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3709514 | pubmed:pagination | 251-7 | lld:pubmed |
| pubmed-article:3709514 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3709514 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3709514 | pubmed:articleTitle | Caldesmon is an elongated, flexible molecule localized in the actomyosin domains of smooth muscle. | lld:pubmed |
| pubmed-article:3709514 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3709514 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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