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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1986-6-30
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-126155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-139917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-2982671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-2985624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-3510219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-3987897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-4254541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-490648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-574428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-5857104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6092349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6130572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6150036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6209340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6437868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6684120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6768755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6803791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-686359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6894930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-691054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-6946503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-7028278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3709514-7067839
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
251-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3709514-Actins,
pubmed-meshheading:3709514-Actomyosin,
pubmed-meshheading:3709514-Animals,
pubmed-meshheading:3709514-Antibodies,
pubmed-meshheading:3709514-Antigen-Antibody Complex,
pubmed-meshheading:3709514-Calmodulin-Binding Proteins,
pubmed-meshheading:3709514-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3709514-Microscopy, Electron,
pubmed-meshheading:3709514-Muscle, Smooth,
pubmed-meshheading:3709514-Myofibrils,
pubmed-meshheading:3709514-Protein Conformation,
pubmed-meshheading:3709514-Stomach,
pubmed-meshheading:3709514-Swine,
pubmed-meshheading:3709514-Viscosity
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pubmed:year |
1986
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pubmed:articleTitle |
Caldesmon is an elongated, flexible molecule localized in the actomyosin domains of smooth muscle.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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