Tropomyosin is in a reduced state in rabbit psoas muscle

Summary Tropomyosin (Tm) purified from skeletal and cardiac muscle often contains disulfide bonds due to oxidation of cysteine groups that are in close proximity in the coiled-coil structure. Are these disulfide crosslinks present in the muscle or produced by oxidation during preparation? To answer...

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Bibliographic Details
Published in:Journal of muscle research and cell motility 2011-08, Vol.32 (1), p.19-21
Main Authors: Lehrer, Sherwin S., Ly, Socheata, Fuchs, Franklin
Format: Article
Language:English
Subjects:
Animal Anatomy
Animals
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cysteine
Disulfides
Dithionitrobenzoic Acid
Electrophoresis, Polyacrylamide Gel
Heart Failure - metabolism
Histology
Humans
Life Sciences
Morphology
Octoxynol
Oxidation-Reduction
Proteomics
Psoas Muscles - chemistry
Psoas Muscles - metabolism
Rabbits
Rapid Communication
Tropomyosin - chemistry
Tropomyosin - isolation & purification
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Summary:Summary Tropomyosin (Tm) purified from skeletal and cardiac muscle often contains disulfide bonds due to oxidation of cysteine groups that are in close proximity in the coiled-coil structure. Are these disulfide crosslinks present in the muscle or produced by oxidation during preparation? To answer this question we reacted one part of freshly dissected rabbit psoas muscle fibers, which was permeabilized with Triton X-100, with N -ethyl maleimide (NEM) to block cysteine groups and another part with 5,5′-dithiobis(2-nitro benzoate) (DTNB) to facilitate disulfide bond formation by interchain sulfhydryl-disulfide exchange. We found, by high resolution gradient SDS polyacrylamide gels, that the NEM-treated muscle was only composed of uncrosslinked Tm and the DTNB treated muscle was composed of disulfide-crosslinked Tm. This work indicates that Tm exists in a reduced state in rabbit psoas muscle.
ISSN:0142-4319
1573-2657
DOI:10.1007/s10974-011-9249-6