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  A myofibrillar protein of insect muscle related to vertebrate titin connects Z band and A band: Purification and molecular characterization of invertebrate mini-titin.

Nave, R., & Weber, K. (1990). A myofibrillar protein of insect muscle related to vertebrate titin connects Z band and A band: Purification and molecular characterization of invertebrate mini-titin. Journal of Cell Science, 95, 535-544.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-0E0A-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-3045-9
Genre: Journal Article

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 Creators:
Nave, R.1, Author              
Weber, K.1, Author              
Affiliations:
1Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578618              

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 Abstract: We show that myofibrils of insect flight and leg muscle contain a doublet of polypeptides with apparent molecular weights of 700K (K = 10(3) Mr) (Hmp I) and 600K (Hmp II), respectively. In Locusta migratoria high ionic strength extraction solubilizes only Hmp II, which is readily purified in native form. It probably reflects a proteolytic derivative of the non-extractable Hmp I. On the basis of its viscosity radius and sedimentation coefficient, Hmp II has a molecular weight of 600K and seems to consist of a single polypeptide chain. The highly asymmetric structure of the molecule is confirmed by rotary shadowing. The flexible rods have a uniform diameter of 3–4 nm and an average length of 260 nm. Polyclonal antibodies show cross-reactivity between Hmp II and its putative precursor Hmp I. We discuss the similarities and differences between the larger titin I/titin II of vertebrate sarcomeric muscle and the smaller Hmp I/Hmp II of invertebrate muscle and conclude that the latter may reflect a mini-titin. In line with the smaller length, immunoelectron microscopy locates the insect mini-titin to the I band and a very short portion of the A band only, while vertebrate titin is known to connect the Z band to the M band. Mini-titin has also been purified from several other insects including Drosophila. Immunofluorescence microscopy on frozen sections shows that mini-titin is present in the sarcomeric muscles of various species from different invertebrate phyla. These include Annelida, Nematomorpha, Plathelmintha, Nemertea and Nematoda like Ascaris lumbricoides and Caenorhabditis elegans. This wide-spread occurrence of invertebrate mini-titin is confirmed by immunoblotting experiments.

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Language(s): eng - English
 Dates: 1990-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: eDoc: 286424
ISI: A1990DA28000003
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Title: Journal of Cell Science
  Alternative Title : J. Cell Sci.
Source Genre: Journal
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Pages: - Volume / Issue: 95 Sequence Number: - Start / End Page: 535 - 544 Identifier: ISSN: 0021-9533