Mapping of fish myosin light chains by two-dimensional gel electrophoresis.
1. Myosins were prepared from the ordinary muscle of 16 fish species as well as from rabbit fast muscle, and light chain subunits [alkali light chains A1, A2 and DTNB (5,5'-dithio-bis-2-nitrobenzoate) light chain] were separated on two-dimensional gel electrophoresis in combination with isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 2. A1 light chains showed mol. wts ranging from 21,000 to 22,900 and isoelectric points ranging from 4.51 to 4.62. DTNB light chains were spotted in a narrow area, with a mol. wt range of 16,800-17,600 and an isoelectric point range of 4.48-4.55. On the other hand, A2 light chains were most species-specific, with a mol. wt range of 14,000-19,500 and an isoelectric point range of 4.31-4.46. 3. It was suggested that the lower species-specificity in A1 as opposed to A2 is accounted for by the addition of an N-terminal peptide ("difference peptide") in the former. The properties and possible role of this peptide are discussed.
Ochiai
Y
Y
Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, Japan.
Kobayashi
T
T
Watabe
S
S
Hashimoto
K
K
D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes / Q000378:metabolism*; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000032:analysis; D008970:Molecular Weight; D015879:Myosin Subfragments / Q000032:analysis*; D010449:Peptide Mapping / Q000379:methods; D011817:Rabbits; D013045:Species Specificity
D007527:Isoenzymes; D015879:Myosin Subfragments