Preparation of fat replacer utilizing gluten and barley β-glucan and the interaction between them.

Background: Fat replacers prepared from polysaccharides and proteins possess functional properties of both polysaccharides and proteins. In this study, an aqueous system of barley β-glucan (BBG) and gluten was prepared. The interactions between BBG and gluten (with/without extrusion modification) were studied.

Depletion of FKBP does not affect the interaction between isolated ryanodine receptors.

The ryanodine receptors/calcium release channels (RyRs) usually form two dimensional regular lattices in the endoplasmic/sarcoplasmic reticulum membranes. The native RyR is associated with many auxiliary proteins, including FKBP. It has been indicated that FKBP may play a role in the intermolecular interaction and coupled gating of neighboring RyRs.

Modulation of the oligomerization of isolated ryanodine receptors by their functional states.

The calcium release channels/ryanodine receptors (RyRs) usually form two-dimensional regular lattices in the endoplasmic/sarcoplasmic reticulum membranes. However, the function and modulation of the interaction between neighboring RyRs are still unknown. Here, with an in vitro aqueous system, we demonstrate that the interaction between RyRs isolated from skeletal muscle (RyR1s) is modulated by their functional states by using photon correlation spectroscopy and [(3)H]ryanodine binding assay.

Effect of Zn2+ ions on ryanodine binding to sarcoplasmic reticulum of striated muscles in the presence of pyrithione.

Aim: To explore whether the differential effects of Zn2+ on ryanodine binding to the sarcoplasmic reticulum (SR) of skeletal and cardiac muscles resulted from different permeability of the SR to Zn2+.

Methods: [3H]ryanodine binding assays were performed to examine the effect of Zn2+ on ryanodine binding to the SR in the presence of pyrithione sodium (PyNa), a specific Zn2+ ionophore.

Results: As a control, PyNa up to 50 micromol/L did not induce any effect on ryanodine binding to the SR of cardiac muscle.

Modulation of the interactions of isolated ryanodine receptors of rabbit skeletal muscle by Na+ and K+.

Ryanodine receptors (RyRs) of skeletal muscle, as calcium release channels, have been found to form semicrystalline arrays in the membrane of sarcoplasmic reticulum. Recently, both experimental observations and theoretical simulations suggested cooperative coupling within interlocking RyRs. To better understand the interactions between RyRs and their modulation, the aggregation and dissociation of isolated RyRs in aqueous medium containing various Na(+) and K(+) concentrations were investigated using photon correlation spectroscopy (PCS) and atomic force microscopy (AFM).

Effect of zinc ions on caffeine-induced contracture in vascular smooth muscle and skeletal muscle of rat.

The effect of zinc ions on caffeine-induced contracture in vascular smooth muscle and skeletal muscle of rat was studied. In aortic strips, caffeine contracture was depressed by Zn2+ in a dose-dependent manner. Moreover, the extent of the depression of caffeine contracture in the Zn2+ loaded smooth muscle increased with repetitive caffeine exposures.