Characterization of the phosphorylatable myosin light chain in rat uterus.

The 20 kDa myosin light chain of 32P-labeled rat uterus exhibited four spots on two-dimensional gel electrophoretograms; the corresponding autoradiograms revealed that three spots were radioactive. Completely dephosphorylated light chain exhibited three spots on electrophoretograms. Serine and threonine residues of the light chain were found to be phosphorylated in the uterus at a ratio of 6 to 1. During contraction, the amount of each phosphoamino acid increased proportionally to the increase in the total phosphate content of the light chain.