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Tropomyosin is a te...
Tropomyosin is a tetramer under physiological salt conditions.
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- Lassing, Ingrid (author)
- Stockholms universitet,Avdelningen för cellbiologi
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- Hillberg, Louise (author)
- Karolinska institutet
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- Höglund, Anna-Stina (author)
- Stockholms universitet,Wenner-Grens institut
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- Karlsson, Roger (author)
- Stockholms universitet,Avdelningen för cellbiologi
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- Schutt, Clarence (author)
- Princeton University
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- Lindberg, Uno (author)
- Stockholms universitet,Wenner-Grens institut
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(creator_code:org_t)
- 2010-08-12
- 2010
- English.
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In: Cytoskeleton (Hoboken, N.J.). - : Wiley. - 1949-3592 .- 1949-3584. ; 67:9, s. 599-607
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Tropomyosin (TM) is a coiled-coil dimer of alpha-helical peptides, which self associates in a head- to-tail fashion along actin polymers, conferring stability to the microfilaments and serving a regulatory function in acto-myosin driven force generation. While the major amount of TM is associated with filaments also in non-muscle cells, it was recently reported that there are isoform-specific pools of TM multimers (not associated with F-actin), which appear to be utilized during actin polymerization and reformed during depolymerization. To determine the size of these multimers, skeletal muscle TM was studied under different salt conditions using gel-filtration and sucrose gradient sedimentation, and compared with purified non-muscle TM 1 and 5, as well as with TM present in non-muscle cell extracts and skeletal muscle TM added to such extracts. Under physiological salt conditions TM appears as a single homogenous peak with the Stokes radius 8.2 nm and the molecular weight (mw) 130,000. The corresponding values for TM 5 are 7.7 nm and 104,000, respectively. This equals four peptides, implying that native TM is a tetramer in physiological salt. It is therefore concluded that the TM multimers are tetramers.
Subject headings
- NATURVETENSKAP -- Biologi -- Cellbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Cell Biology (hsv//eng)
Keyword
- tropomyosin assembly;ionic strength dependence;microfilament organization;actin polymerization;cell motility
Publication and Content Type
- ref (subject category)
- art (subject category)
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