ITP induces superprecipitation of skeletal acto-gizzard myosin in a pH- and phosphorylation-dependent manner, despite not serving as a substrate for myosin light-chain kinase.
Hypothesis-generating for pH-dependent myosin regulation; leaves open physiological relevance in intact muscle.
Inosine triphosphate (ITP) does not serve as a substrate for myosin light-chain kinase from gizzard muscle. That is to say, myosin light-chain is not phosphorylated in ITP media. Nevertheless, at pH 6.8, 1 mM or 5 mM ITP induces superprecipitation of skeletal acto-gizzard myosin. The ITP-induced superprecipitation occurs in the absence or presence of calcium ions, and regardless of whether gizzard myosin is phosphorylated or not. On the other hand, at pH 8, 5 MM ITP induces practically no superprecipitation of skeletal acto-gizzard unphosphorylated myosin, whereas it does induce a strong superprecipitation of skeletal acto-gizzard phosphorylated myosin. Superprecipitation is also independent of the presence or absence of calcium ions.
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Onishi et al. (1979) studied this question.
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