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The Journal of Cell Biology, Vol 55, 586-594, Copyright © 1972 by Rockefeller University Press

ARTICLE

SOME PROPERTIES OF EMBRYONIC MYOSIN

F. Sreter 1, S. Holtzer 1, J. Gergely 1, and H. Holtzer 1

1 From the Department of Muscle Research, Boston Biomedical Research Institute, Boston Massachusetts 02114; the Department of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114; the Department of Biological Chemistry, Harvard Medical School, Cambridge, Massachusetts 02138; and the Department of Anatomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104

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.

Submitted on June 19, 1972
Revised on July 31, 1972


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