Abstract
IT is generally accepted that myosin in vertebrate fast-twitch and slow-twitch muscles is structurally1–4 and immunochemically5–8 distinct and exists in several isoenzymatic forms9–14. The nature of myosin in developing mammalian skeletal muscles is controversial. Some authors15,16 consider it to be identical to adult fast-twitch myosin on the basis of light-chain composition and histochemistry. Others8 suggest that it may be a mixture of fast-twitch and slow-twitch myosins. Still others4,17 maintain it is a distinct fetal form of myosin differing in primary structure from adult myosins. In this report we show that (1) myosin in both neonatal and adult fast-twitch muscles of the rabbit exists in three electrophoretically distinct isoenzymatic forms which differ in light-chain composition, and (2) the two-dimensional peptide map of the heavy chains of neonatal muscle myosin is distinct from maps of both fast-twitch and slow-twitch myosins. These results clearly establish the existence of fetal myosin isoenzymes in developing mammalian muscles and resolve apparent contradictions in the literature.
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HOH, J., YEOH, G. Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles. Nature 280, 321–323 (1979). https://doi.org/10.1038/280321a0
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DOI: https://doi.org/10.1038/280321a0
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