| Literature DB >> 21136625 |
Ruud Zaremba1, Daphne Merkus, Nazha Hamdani, Jos M J Lamers, Walter J Paulus, Cris Dos Remedios, Dirk J Duncker, Ger J M Stienen, Jolanda van der Velden.
Abstract
Phosphorylation of cardiac myofilament proteins represents one of the main post-translational mechanisms that regulate cardiac pump function. Human studies are often limited by the amount of available tissue as biopsies taken during cardiac catheterization weigh only 1 mg (dry weight). Similarly, investigation of time- (or dose-) dependent changes in protein phosphorylation in animal studies is often hampered by tissue availability. The present study describes quantitative analysis of phosphorylation status of multiple myofilament proteins by 2-DE and Pro-Q® Diamond stained gradient gels using minor amounts (˜0.5 mg dry weight) of human and pig cardiac tissue.Entities:
Year: 2007 PMID: 21136625 DOI: 10.1002/prca.200600891
Source DB: PubMed Journal: Proteomics Clin Appl ISSN: 1862-8346 Impact factor: 3.494