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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1989-9-28
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pubmed:abstractText |
The microsomal fraction of normal human skeletal muscle was subfractionated by isopycnic sucrose-density centrifugation, using the procedure originally described by Saito et al. for rabbit fast muscle, and specific markers of the junctional face membrane of terminal cisternae (TC) (ryanodine receptor, high-molecular-weight feet proteins and membrane-associated calcium-binding protein calsequestrin), of the sarcoplasmic reticulum (SR) Ca-pump membrane (chicken antibody to rabbit Ca-ATPase), and of transverse tubules (TT) (dihydropiridine receptor, membrane cholesterol), respectively. The results show that isolated TC from human skeletal muscle share extensive morphological characteristics, protein composition, as well as Ca-release properties with rabbit TC, as tested with an inhibitor (Ruthenium red) and an activator (doxorubicin) of SR Ca-release. The Ca-pump membrane of human muscle SR, in distinction to rabbit fast muscle SR, showed a relatively low specific activity of the Ca-ATPase, as expected from the mixed fiber composition of human muscles, but shared the presence of minor protein components, such as a Con A binding protein of about 57 kDa and blue-staining peptides in the 170-120 kDa range of molecular weights. Human muscle TT, as isolated from the same sucrose gradient, demonstrated a high affinity (3H)-dihydropiridine binding activity in the range of previously reported values for purified TT from rabbit skeletal muscle.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0148-639X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
323-31
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2549416-Blotting, Western,
pubmed-meshheading:2549416-Calcium Channels,
pubmed-meshheading:2549416-Calcium-Transporting ATPases,
pubmed-meshheading:2549416-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2549416-Humans,
pubmed-meshheading:2549416-Microscopy, Electron,
pubmed-meshheading:2549416-Muscle Proteins,
pubmed-meshheading:2549416-Muscles,
pubmed-meshheading:2549416-Sarcoplasmic Reticulum,
pubmed-meshheading:2549416-Subcellular Fractions
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pubmed:year |
1989
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pubmed:articleTitle |
Biochemical characteristics of free and junctional sarcoplasmic reticulum and of transverse tubules in human skeletal muscle.
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pubmed:affiliation |
National Research Council Center for Muscle Biology and Physiopathology, Institute of General Pathology, Padova, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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