1. Studies on the subunits of myosin from muscle layer of Ascaris lumbricoides suum.
- Author
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Nakamura T, Yanagisawa T, and Yamaguchi M
- Subjects
- Adenosine Triphosphatases metabolism, Chemical Precipitation, Dithionitrobenzoic Acid, Dithiothreitol, Molecular Weight, Myosins isolation & purification, Peptide Fragments analysis, Urea, Ascaris analysis, Muscles analysis, Myosins analysis
- Abstract
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.
- Published
- 1975
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