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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-5-1
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pubmed:abstractText |
A simplified procedure to isolate alpha-connectin (titin 1, TI), a gigantic elastic protein, from rabbit skeletal muscle is described. A rapid column chromatography step to concentrate alpha-connectin is introduced. Separation of alpha-connectin from beta-connectin is introduced. Separation of alpha-connectin from beta-connectin (titin 2, TII) in the presence of 4 M urea at pH 7.0 did not cause any change in the secondary structure of alpha-connectin as judged by circular dichroic spectra. Ultraviolet absorption spectra and the amino acid composition of alpha-connectin (MW, approximately 3 x 10(6)) were similar to those of its proteolytic product, beta-connectin (MW, approximately 2 x 10(6)). Circular dichroic spectra suggested that both alpha- and beta-connectin consist of 60% beta-sheet and 30% beta-turn. It thus appears that the whole elastic filament of connectin has a folded beta-strand structure. Proteolysis of alpha-connectin by calpain resulted in formation of beta-connectin and smaller peptides. The alpha-connectin interacted with both myosin and actin filaments similarly to beta-connectin. Polyclonal antibodies raised against 1200 kDa peptides obtained from aged rabbit skeletal myofibrils reacted with alpha-connectin (titin 1, TI) but only weakly with beta-connectin (titin 2, TII) in rabbit skeletal muscle. Immunoelectron microscopy and indirect immunofluorescence microscopy revealed that the antibodies bound at the Z-line and at the epitope regions in the I-band near the binding site of a monoclonal antibody SM1 whose position depends on sarcomere length. It thus appears that beta-connectin extends from the edge of M-line to the above epitope region in the I-band.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Elastin,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/connectin
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0142-4319
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-47
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1556169-Actins,
pubmed-meshheading:1556169-Amino Acids,
pubmed-meshheading:1556169-Animals,
pubmed-meshheading:1556169-Antibodies,
pubmed-meshheading:1556169-Elastin,
pubmed-meshheading:1556169-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1556169-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:1556169-Fluorescent Antibody Technique,
pubmed-meshheading:1556169-Immunoblotting,
pubmed-meshheading:1556169-Microscopy, Immunoelectron,
pubmed-meshheading:1556169-Muscle Proteins,
pubmed-meshheading:1556169-Muscles,
pubmed-meshheading:1556169-Myosins,
pubmed-meshheading:1556169-Protein Kinases,
pubmed-meshheading:1556169-Rabbits
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pubmed:year |
1992
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pubmed:articleTitle |
Characterization and localization of alpha-connectin (titin 1): an elastic protein isolated from rabbit skeletal muscle.
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pubmed:affiliation |
Department of Biology, Faculty of Science, Chiba University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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