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The primary structure of skeletal muscle myosin heavy chain: I. Sequence of the amino-terminal 23 kDa fragment.
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- Author(s): Hayashida M;Hayashida M; Maita T; Matsuda G
- Source:
Journal of biochemistry [J Biochem] 1991 Jul; Vol. 110 (1), pp. 54-9.
- Publication Type:
Comparative Study; Journal Article
- Language:
English
- Additional Information
- Source:
Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Print ISSN: 0021-924X (Print) Linking ISSN: 0021924X NLM ISO Abbreviation: J Biochem Subsets: MEDLINE
- Publication Information:
Publication: : Abingdon, UK : Oxford University Press
Original Publication: Tokyo : Japanese Biochemical Society
- Subject Terms:
- Abstract:
Subfragment-1 was prepared from adult chicken pectoralis myosin by limited digestion with alpha-chymotrypsin, and an amino-terminal 23 kDa fragment of the heavy chain was obtained by digesting the subfragment-1 with trypsin. The 205-residue sequence of the fragment was determined by sequencing its cyanogen bromide, tryptic, and chymotryptic peptides. The amino-terminal alpha-amino group of the fragment was acetylated, and two methylated lysines; epsilon-N-monomethyllysine and epsilon-N-trimethyllysine were recognized at the 35th and 130th positions, respectively, as in rabbit skeletal myosin. Comparing the 205-residue sequence of the skeletal myosin with those of cardiac, and gizzard myosins from chicken, considerable differences are recognized, especially in the amino-terminal region, but strong homologies are observed around the reactive lysine residue, around the epsilon-N-trimethyllysine residue, and around the consensus sequence of GXXGXGKT for nucleotide-binding proteins. On the other hand, only 12 amino acid substitutions are recognized between adult and embryonic skeletal myosins, allowing for the post-translational methylation.
- Accession Number:
0 (Amino Acids)
0 (Myosin Subfragments)
EC 3.6.4.1 (Myosins)
- Publication Date:
Date Created: 19910701 Date Completed: 19911206 Latest Revision: 20190510
- Publication Date:
20231215
- Accession Number:
10.1093/oxfordjournals.jbchem.a123543
- Accession Number:
1939027
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