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  Protein chemical analysis of purified murine lamin B identifies two distinct polypeptides B1 and B2.

Weber, K., Plessmann, U., & Traub, P. (1990). Protein chemical analysis of purified murine lamin B identifies two distinct polypeptides B1 and B2. FEBS Letters, 261(2), 361-364. doi:10.1016/0014-5793(90)80592-7.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-0E34-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-37CA-9
Genre: Journal Article

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603039.pdf (Publisher version), 566KB
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 Creators:
Weber, K.1, Author              
Plessmann, U.2, Author              
Traub, P., Author
Affiliations:
1Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578618              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Lamin B purified from murine EAT cells was characterized by partial protein sequences. Contrary to the current view that mammals express only a single lamin B polypeptide corresponding to a characterized murine cDNA clone, our analysis documents two distinct B lamins. One protein follows the estabished cDNA sequence while the other identifies a novel murine lamin B. Comparison with the two chicken lamin B sequences established by cDNA cloning identifies the first murine lamin B sequence as a B1 type and the second as a B2 type. We conclude that mammals express two distinct lamin B forms as established by others for chicken.

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Language(s): eng - English
 Dates: 1990-02-26
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 261 (2) Sequence Number: - Start / End Page: 361 - 364 Identifier: ISSN: 0014-5793