Abstract
Myosins from the following sources were purified by diethylaminoethyl-Sephadex chromatography: moytubes grown in vitro for 7-8 days, prepared from pectoralis muscles of 10-day old embryos, and breast and leg muscles from 16-day old embryos. The adenosine triphosphatase activities of these myosins were close to that of adult m. pectoralis myosin. The light chains of the embryonic myosins had the same mobilities in sodium dodecyl sulfate electrophoresis as those in adult pectoralis muscle myosin and were clearly distinguishable from those in myosin from tonic muscle m. latissimus dorsi anterior. The fastest light chain in embryonic muscle myosin-apparent mol wt 16,000-was present in smaller amounts than in adult myosin. The negative staining pattern of paracrystals of embryonic light meromyosin (LMM) was indistinguishable from that of adult fast muscle LMM. The significance of these results for differentiation of various muscle types has been discussed.
MeSH Terms
Adenosine Triphosphatases/analysis
Animals
Chick Embryo
Chromatography, Ion Exchange
Culture Techniques
Electrophoresis, Polyacrylamide Gel
Macromolecular Substances
Microscopy, Electron
Muscle Development
Muscles/embryology,enzymology
Myosin Subfragments
Myosins/analysis,isolation & purification
Sodium Dodecyl Sulfate
Staining and Labeling
Chemicals
Macromolecular Substances
Myosin Subfragments
Sodium Dodecyl Sulfate
Adenosine Triphosphatases
Myosins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sreter F
Holtzer S
Gergely J
Holtzer H
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19 references, click to expand
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