Calcium Regulation in Chicken Gizzard Muscle and Inosine Triphosphate-Induced Superprecipitation of Skeletal Acto-Gizzard Myosin
- 1 August 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 86 (2) , 569-573
- https://doi.org/10.1093/oxfordjournals.jbchem.a132556
Abstract
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.Keywords
This publication has 2 references indexed in Scilit:
- Purification and properties of myosin light-chain kinase from fast skeletal muscleBiochemical Journal, 1977
- The effect of phosphorylation of gizzard myosin on actin activationBiochemical and Biophysical Research Communications, 1976