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. 1984 Mar 15;218(3):841–847. doi: 10.1042/bj2180841

Phosphorylation in vivo of the P light chain of myosin in rabbit fast and slow skeletal muscles.

S A Westwood, O Hudlicka, S V Perry
PMCID: PMC1153413  PMID: 6721836

Abstract

The P light chain of myosin is partially phosphorylated in resting slow and fast twitch skeletal muscles of the rabbit in vivo. The extent of P light-chain phosphorylation increases in both muscles on stimulation. Rabbit slow-twitch muscles contain two forms of the P light chain that migrate with the same electrophoretic mobilities as the two forms of P light chain in rabbit ventricular muscle. The rate of phosphorylation of the P light chain in slow-twitch muscle is slower than its rate of phosphorylation in fast-twitch muscles during tetanus. The rate of P light-chain dephosphorylation is slow after tetanic contraction of fast-twitch muscles in vivo. The time course of dephosphorylation does not correlate with the decline of post-tetanic potentiation of peak twitch tension in rabbit fast-twitch muscles. The frequency of stimulation is an important factor in determining the extent of P light-chain phosphorylation in fast- and slow-twitch muscles.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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