English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

In this study, the effect of glyceraldehyde 3-phosphate dehydrogenase (G3PD) on the molecular state of porcine myofibrils was investigated by observing the structural changes in myosin and actin in myofibrils using phasecontrast and fluorescence microscopy. Though the myofibril gel strength was not influenced by G3PD at a G3PD to myofibril weight ratio (G/M ratio) of 1/20, the gel strength significantly increased at a G/M ratio ≥ 1/10. SDS-PAGE analysis demonstrated that myosin heavy chain band intensity increased in the myofibril soluble fraction by adding G3PD, suggesting G3PD facilitated the solubilization of myosin and actin. Phase-contrast microscopy also showed increased myofibril solubilization with increasing G3PD. Fluorescence microscopy revealed that G3PD colocalized with actin segments. Myosin segments also colocalized with actin segments in G3PD-treated myofibrils, suggesting myosin bound to actin. The addition of G3PD to myofibrils increased the Mgand Mg-EGTA-ATPase activities, suggesting G3PD would not change the conformation of myofibrils.

Evaluation of the Effect of Glyceraldehyde 3-phosphate Dehydrogenase on Heat-induced Myofibril Gels by Investigating Actin-myosin Interaction