Physicochemical and immunological properties of myosin light chains from the ordinary muscle of marine teleost fishes.
1. Myosin light chains (A1, A2 and DTNB light chain) were isolated from the ordinary muscle of six marine fishes and the physicochemical and immunological properties were examined. 2. All the isolated light chains were rich in aspartic and glutamic acids, alanine and lysine, but poor in histidine and tyrosine. The contents of alanine, proline and lysine were generally higher in A1 than in A2. Between closely related species such as skipjack and bonito, the amino acid profiles of corresponding light chains were very similar to each other. 3. Structural similarity and difference of A1 light chain were further demonstrated immunologically using anti-A1 antiserum. Precipitation lines were fused with each other among closely related species, whereas strong spurs were observed among phylogenetically distinct species.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes / Q000378:metabolism*; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D009132:Muscles / Q000032:analysis; D015879:Myosin Subfragments; D009218:Myosins / Q000276:immunology / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000276:immunology / Q000302:isolation & purification*; D013045:Species Specificity; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D015879:Myosin Subfragments; D010446:Peptide Fragments; D009218:Myosins