Amino Acid Sequence of the Essential Light Chain of Adductor Muscle Myosin from Ezo Giant Scallop, Patinopecten yessoensis

• Published in: Journal of biochemistry (Tokyo) 1987-11, Vol.102 (5), p.1141-1149
• Main Authors: MAITA, Tetsuo, KONNO, Kunihiko, MARUTA, Shinsaku, NORISUE, Hajime, MATSUDA, Genji
• Format: Article
• Language: English
• Subjects: adductor muscle; Amino Acid Sequence; amino acids; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chromatography; Chymotrypsin; Contractile proteins; Fundamental and applied biological sciences. Psychology; Holoproteins; Marine; Molecular Sequence Data; Mollusca - metabolism; Muscles - analysis; Myosins; Patinopecten yessoensis; Pepsin A; Peptide Fragments - isolation & purification; Proteins; Sequence Homology, Nucleic Acid; Trypsin
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a122152

The amino acid sequence of the essential light chain (abbreviated as SHLC) of adductor muscle myosin from Ezo giant scallop (Patinopecten yessoensis) was determined by conventional methods. The light chain was composed of 156 amino acid residues with proline and lysine as its amino and carboxyl termini, respectively. Comparing this sequence with that of the SHLC from bay scallop (Aquipecten irradians), only 5 amino acid substitutions were recognized. The sequence homology between scallop and squid SHLCs was 53.7%. On the other hand, a partially fragmented SHLC “modified SHLC” reported by Konno and Watanabe (J. Biochem. 98, 141–148 (1985)) was prepared by chymotryptic digestion of the scallop myosin in the presence of EDTA, and was assigned as the carboxyl-terminal 106-residue peptide of the SHLC. This may suggest that the regulatory light chain covers the amino-terminal region of the SHLC in the myosin molecule.