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  Repetitive titin epitopes with a 42 nm spacing coincide in relative position with known A band striations also identified by major myosin-associated proteins. An immunoelectron-microscopical study on myofibrils.

Fürst, D., Nave, R., Osborn, M., & Weber, K. (1989). Repetitive titin epitopes with a 42 nm spacing coincide in relative position with known A band striations also identified by major myosin-associated proteins. An immunoelectron-microscopical study on myofibrils. Journal of Cell Science, 94, 119-125.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2F1B-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2F1E-A
Genre: Journal Article

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Fürst, D.1, Author              
Nave, R.1, Author              
Osborn, M.1, Author              
Weber, K.1, Author              
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1Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578618              

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 Abstract: A direct titin-thick filament interaction in certain regions of the A band is suggested by results using four new monoclonal antibodies specific for titin in immunoelectron microscopy. Antibodies T30, T31 and T32 identify quasi-repeats in the titin molecule characterized by a 42–43 nm repeat spacing. These stripes seem to coincide with striations established by others on negatively stained cryosections of the A band. Antibodies T30 and T32 recognize epitopes matching five or two of the seven striations per half sacromere known to harbor both the myosin-associated C-protein and an 86K (K = 10(3) Mr) protein. Antibody T31 labels two stripes in the P zone, which correspond to the two positions where decoration is seen with 86K protein, but not with C-protein. The single titin epitope defined by antibody T33 is located 55 nm prior to the center of the M band. This position seems to coincide with the M7 striation defined by others on negatively stained A bands. The T33 epitope position proves that the titin molecule, which is known to be anchored at the Z line, also penetrates into the complex architecture of the M band. The titin epitopes described here enable us to begin to correlate known ultrastructural aspects of the interior part of the A band with the disposition of the titin molecule in the sarcomere. They raise the question of whether there is a regular interaction pattern between titin and the thick filaments.

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Language(s): eng - English
 Dates: 1989-09
 Publication Status: Published in print
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Title: Journal of Cell Science
Source Genre: Journal
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Pages: - Volume / Issue: 94 Sequence Number: - Start / End Page: 119 - 125 Identifier: -