The Amino Acid Sequence of the L-2 Light Chain of Chicken Skeletal Muscle Myosin

Suzuyama, Yoji; Umegane, Toshiyo; Maita, Tetsuo; Matsuda, Genji

doi:10.1515/bchm2.1980.361.1.119

Cited by 23 publications

(3 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results suggest that the spectral changes regarding the Tyr and Phe residues are restricted to myosin. According to the primary structure information of myosin (Suzuyama et al, 1980;, ∼90% of total Tyr residues and ∼80% of total Phe residues contribute to S-1. Thus, the changes in the Tyr and Phe bands appearing in the Raman spectra are mainly derived from S-1 portion.…”

Section: Discussionmentioning

confidence: 99%

Raman Spectroscopic Study of Changes in Fish Actomyosin during Setting

Ogawa

Nakamura

Horimoto

et al. 1999

J. Agric. Food Chem.

View full text Add to dashboard Cite

Actomyosins (AMs) isolated from tilapia, lemon sole, ling cod, and rock fish were heated at 40 degrees C, and structural changes in AMs were investigated using Raman spectroscopy to elucidate low-temperature gelling phenomenon, that is, "setting", of surimi. The following conformational transitions were observed in lemon sole, ling cod, and rock fish gels during setting: a slow unfolding of alpha-helix and exposure of hydrophobic amino acid residues occurring in long-time incubation at 40 degrees C, thereby forming hydrophobic interactions among AM molecules. In addition, the most frequent conformation in disulfide bonds was gauche-gauche-trans (g-g-t) form in the set gel. On the other hand, tilapia AM did not form a gel with heating at 40 degrees C, its alpha-helical structure in the myosin being far more stable than that of the other species. The heat resistance of the tight alpha-helix may prevent the gelation of tilapia AM. It is, therefore, likely that the unfolding of the alpha-helix of myosin is a prerequisite for gelation of AM during setting.

show abstract

Section: Discussionmentioning

confidence: 99%

Raman Spectroscopic Study of Changes in Fish Actomyosin during Setting

Ogawa

Nakamura

Horimoto

et al. 1999

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…The following is the list of accession numbers for the skeletal MLC2 sequences. Mammalian: P41691, Felis catus superfast MLC2 (Qin et al, 1994); Q02045, Homo sapiens superfast MLC2 (Collins et al, 1992); P24732, Oryctolagus cuniculus (Maeda et al, 1990); P04466, Rattus norvegicus (Nudel et al, 1984); P97457, Mus musculus (Palermo et al, 1995); Avian: P02609, Gallus gallus (Suzuyama et al, 1980); Piscine: AAF71271, Oncorhynchus kisutch (Hill et al, 2000); AAC32193, Danio rerio (Xu et al, 1999); AAF00097, Danio rerio cardiac MLC2 (Yelon et al, 1999) (Hirayama et al, 1998).…”

Section: Phylogenetic Analysismentioning

confidence: 99%

Molecular cloning and sequence of Sparus aurata skeletal myosin light chains expressed in white muscle: developmental expression and thyroid regulation

Moutou¹,

Power²,

Canário³

1999

Comparative Biochemistry and Physiology Part A: Molecular &

View full text Add to dashboard Cite

“…Adult rat skeletal muscle contains three light chains of molecular weight 23,000 (MLC1), 17,000 (MLC2), and 15,000 (MLC3) (7). The amino acid sequence of skeletal muscle MLC2 has been determined for rabbit (8), and chicken (9). Chicken contains at least three other MLC2 polypeptides, two in cardiac muscle (L2A and L2B) and one in gizzard (10).…”

Section: Introductionmentioning

confidence: 99%

The nucleotide sequence of a rat myosin light chain 2 gene

et al. 1984

View full text Add to dashboard Cite

A rat myosin light chain 2 gene was characterized by nucleotide sequence and S1 mapping analyses. It contains seven exons separated by six introns. The corresponding mRNA is predicted to be 654 nucleotides long (excluding polyA sequences), with 5'-nontranslated, coding, and 3'-nontranslated lengths of 56, 510, and 88 nucleotides, respectively. The predicted amino acid sequence is identical to that from rabbit except that the rat sequence lacks one of two Gly residues located at positions 12 and 13 in the rabbit sequence. From the nucleotide sequence, nascent rat myosin light chain 2 is predicted to have Met Ala preceding Pro at the N-terminal end.

show abstract

The Amino Acid Sequence of the L-2 Light Chain of Chicken Skeletal Muscle Myosin

Cited by 23 publications

References 6 publications

Raman Spectroscopic Study of Changes in Fish Actomyosin during Setting

Raman Spectroscopic Study of Changes in Fish Actomyosin during Setting

Molecular cloning and sequence of Sparus aurata skeletal myosin light chains expressed in white muscle: developmental expression and thyroid regulation

The nucleotide sequence of a rat myosin light chain 2 gene

Contact Info

Product

Resources

About