Analysis of Smooth Muscle Myosin Phosphorylation with Native Pyrophosphate Gels and Its Application to Studies on Myosin Phosphorylation in Contracting Smooth Muscle1
- 1 October 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 100 (6) , 1681-1684
- https://doi.org/10.1093/oxfordjournals.jbchem.a121878
Abstract
Gizzard smooth muscle myosin, the 20,000 Mr light chain (L20) of which had been phosphorylated in vitro with a calmodulin-myosin light chain kinase system, was separated into 5 isolated bands in a pyrophosphate polyacrylamide gel. Their mobilities were in the following order: myosin with 2 unphosphorylated L20 (GM) < myosin with 1 unphosphorylated and 1 mono-phosphorylated L20 (GMP1) < myosin with 2 mono-phosphorylated L20 (GMP2) < myosin with 1 mono-phosphorylated and 1 di-phosphorylated L20 (GMP3) < myosin with 2 di-phosphorylated L20 (GMP4). We used this pyrophosphate polyacrylamide gel electrophoresis to analyze the phosphorylated state of taenia coli smooth muscle during K+-induced contraction. During the initial 2 nun contraction, phosphorylated forms corresponding to GMP1 and GMP2 were detected in addition to the unphosphorylated form.This publication has 0 references indexed in Scilit: