Amino acid sequences were analyzed for two isoforms of myosin essential light chain, LC17a and LC17b [Hasegawa. Y., Ueno, H., Hone, K., & Morit.a F. (1988) J. Biochem. 103, 15-18] from porcine aorta smooth muscle. Both LC17a and LC17b consisted of 150 amino acid residues and their N-terminal Cys residues were blocked by an acetyl group. The amino acid sequences of LC17a and LC17b were common from the N-terminal to Glu-141 and five amino acid substitutions were observed within the remaining C-terminal 9 residues. The amino acid sequences of LC17a and LC17b were identical to those deduced from the nucleotide sequences of bovine aortic cDNAs encoding the two isoforms [Lash, J. A., Helper, D.J., Kiug, M., Nicolozakes, A.W., & Hathaway, D.R. (1990) Nucleic Acids Res. 18, 7176].
|Number of pages||6|
|Journal||Journal of biochemistry|
|Publication status||Published - 1992 Jun|
ASJC Scopus subject areas
- Molecular Biology