Comparative gel-based proteomic analysis of chemically crosslinked complexes in dystrophic skeletal muscle.

ABSTRACT: Duchenne muscular dystrophy is a highly progressive muscle wasting disease with a complex pathophysiology that is based on primary abnormalities in the dystrophin gene. In order to study potential changes in the oligomerization of high-molecular-mass protein complexes in dystrophic skeletal muscle, chemical crosslinking was combined with mass spectrometric analysis. The biochemical stabilization of protein interactions was carried out with the homo-bifunctional and amine-reactive agent bis[sulfosuccinimidyl]suberate, followed by protein shift analysis in one-dimensional gels. The proteomic approach identified 11 and 15 protein species in wild type versus dystrophic microsomal fractions, respectively, as well as eight common proteins, with an electrophoretic mobility shift to very high mole

SUBMITTER: Murphy S 

PROVIDER: S-EPMC6099379 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature