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- W2009408092 abstract "Abstract The different speeds of contraction of slow-twitch and fast-twitch mammalian hind limb muscles correlate with their myosin ATPase activities. Consequently, the structural characterization of these two types of myosin is relevant to an examination of the genetic level at which the speed of contraction is controlled. The myosin molecule consists of two to four light chains (molecular weight approx, 20,000), and two heavy chains (molecular weight of 200,000 each). The light chains from fast and slow muscle myosin are known to differ in number and molecular weight. Tryptic digestion of cat gastrocnemius (a fast muscle) myosin revealed a distinct peptide band of 88,000 daltons in sodium dodecyl sulfate-gel electrophoresis. This peptide was altogether absent in tryptic digests of cat soleus (a slow muscle) myosin. This difference in heavy chains from the two types of myosin was still evident after removing the light chains with p -chloromercuriphenyl sulfonate. The fast muscle myosin heavy chain still retained its characteristic peptide band, but its molecular weight had decreased to 77,000. Thus, the myosins from fast and slow muscles are different with respect to heavy chains (as well as light chains). It is therefore suggested that two different sets of genes are responsible for the synthesis of heavy chains in fast and slow muscles." @default.
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- W2009408092 date "1975-12-01" @default.
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- W2009408092 title "Differences between the heavy chains of fast and slow muscle myosin" @default.
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- W2009408092 doi "https://doi.org/10.1016/0014-4886(75)90056-4" @default.
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