Studies on the subunits of myosin from muscle layer of Ascaris lumbricoides suum.
1. A purified preparation of Ascaris myosin was obtained from the muscle layer of Ascaris lumbricoides suum, using gel filtration and ion-exchange chromatography. 2. Ascaris myosin whether purified or unpurified, had almost the same ability for ATP-splitting and superprecipitation. 3. Ascaris myosin and rabbit skeletal myosin were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A significant difference in the number of light chains between both myosins was found. Ascaris myosin was found to have one heavy chain and two distinct light chain components (LC1-A and LC2-A), having molecular weights of 18000 and 16000, respectively. These light chains correspond in molecular weight to the light chain 2 (LC2-S) and light chain 3 (LC3-S) in rabbit skeletal myosin. 4. LC1-A could be liberated from the Ascaris myosin molecule reacted with 5,5'-dithio-bis(2-nirobenzoic acid( Nbs2) with recovery of ATPase activity by addition of dithiothreitol. These properties are equivalent to those of the LC2-S in rabbit skeletal myosin, although Ascaris myosin when treated with Nbs2-urea lost its ATPase activity.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001200:Ascaris / Q000032:analysis*; D011232:Chemical Precipitation; D004228:Dithionitrobenzoic Acid; D004229:Dithiothreitol; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis*; D009218:Myosins / Q000032:analysis* / Q000302:isolation & purification; D010446:Peptide Fragments / Q000032:analysis; D014508:Urea
D010446:Peptide Fragments; D014508:Urea; D004228:Dithionitrobenzoic Acid; D000251:Adenosine Triphosphatases; D009218:Myosins; D004229:Dithiothreitol