POLYACRYLAMIDE-GEL ELECTROPHORETIC METHODS IN THE SEPARATION OF STRUCTURAL MUSCLE PROTEINS

Citation
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
Citations number
180
Categorie Soggetti
Chemistry Analytical
Journal title
Volume
698
Issue
1-2
Year of publication
1995
Pages
301 - 332
Database
ISI
SICI code
Abstract
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.