Abstract
MYOSIN from vertebrate skeletal muscles contains four low molecular weight subunits which are thought to play a functional role in the enzymic activity of myosin1,2 Removal of ‘alkali light chains’ (21,000 and 17,000 g mol−1) results in complete loss of ATPase activity, but dissociation of ‘DTNB light chain’ (18,000 g mol−1) leaves the enzymic activity of myosin essentially unaffected3–6. Since harsh solvents are required to dissociate alkali light chains from heavy chains (as the name implies), it is unclear whether the activity loss is related primarily to denaturation of the heavy chain or to removal of the light chain7.
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MARGOSSIAN, S., LOWEY, S. & BARSHOP, B. Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actin. Nature 258, 163–166 (1975). https://doi.org/10.1038/258163a0
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DOI: https://doi.org/10.1038/258163a0
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