K. Barany et al., POLYACRYLAMIDE-GEL ELECTROPHORETIC METHODS IN THE SEPARATION OF STRUCTURAL MUSCLE PROTEINS, Journal of chromatography, 698(1-2), 1995, pp. 301-332
Polyacrylamide gel electrophoresis plays a major role in analyzing the
function of muscle structural proteins. This review describes one- an
d two-dimensional gel electrophoretic methods for qualitative and quan
titative investigation of the muscle proteins, with special emphasis o
n determination of protein phosphorylation. The electrophoretic studie
s established the subunit structures of the muscle proteins, character
ized their multiple forms, revealed changes in subunit composition or
shifts in isoform distribution of specific proteins during development
, upon stimulation or denervation of the muscle. Protein phosphorylati
on during muscle contraction is preferentially studied by two-dimensio
nal gel electrophoresis. The same method demonstrated protein alterati
ons in human neuromuscular diseases.