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- W2116769495 abstract "Phosphorylation of the 20,000 Mr light chain (L 20 ) of gizzard myosin reversibly increased the mobility of myosin in pyrophosphate polyacrylamide gel electrophoresis (PP 1 PAGE). Gizzard heavy meromyosin (HMM) with phosphorylated L 20 also moved faster than that with unphosphorylated L 20 . This mobility increase of HMM is large enough to account for that of intact myosin. Scallop myosin, desensitized by removing its regulatory light chain, was combined with L 20 and subjected to PP 20 PAGE. Hybrid myosin with the phosphorylated light chain moved faster than that with the unphosphorylated light chain. No such effect of light chain phosphorylation was observed with phosphorylatable light chain from breast or ventricular myosin. Thus, gizzard, but not breast or ventricular phosphorylatable light chain is furnished with the regulatory property that its phosphorylation increases myosin mobility in PP 1 PAGE." @default.
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- W2116769495 date "1986-01-01" @default.
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- W2116769495 title "The Mobility of Gizzard Myosin in Pyrophosphate Gel Electrophoresis Is Increased by Its Light Chain Phosphorylation1" @default.
- W2116769495 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a121711" @default.
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