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

Weber, K.; Plessmann, U.; Traub, P.

doi:10.1016/0014-5793(90)80592-7

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

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Weber, K.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Plessmann, U.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Zitation

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.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0013-0E34-B

Zusammenfassung

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.