Polypropylene/montmorillonite nanocomposites (PPCN) were prepared by melt intercalation with maleic anhydride modified low isotactic polypropylene as the compatibilizer. The linear and nonlinear rheological properties of polypropylene/montmorillonite nanocomposites were studied. The deviation from linear behavior occurred at a strain of 10 0 that was quite less than that for the polymer matrix. The results of dynamic frequency scan showed that the percolation threshold of PPCN was near 3 wt %. Having been subjected to steady preshear, the tactoids could be oriented preferentially in the shear direction, and the percolation network was ruptured. The magnitudes of the stress overshoots observed in the reverse flow experiments were strongly dependent on the rest time, which indicated that the ruptured network could be reorganized even under quiescent conditions. Furthermore, PPCN displayed a strain-scaling stress response to the startup of steady shear. The maxima of the stress overshoots appeared at the stain of 10 0 , which was consistent with the strain where the deviation of linear viscoelastic behavior started. It might imply that subjected to the deformation less than 10 0 , the network structure could be regard as elastic one. Additionally, the analogous strain-scaling stress response to the startup steady shear elucidated the structural analogy between PPCN and liquid crystal polymer solution.
A selenium-containing catalytic antibody (Se-4A4), prepared by converting reactive serine residues of a monoclonal antibody (4A4) raised against a GSH derivative into selenocysteines, acts as a mimic of cytosolic glutathione peroxidase (cGPX). To clarify the mechanism of action of this catalytic antibody, detailed studies on kinetic behaviour and biological activity were carried out. A rate of acceleration (kcat/Km/kuncat) 10(7)-fold that of the uncatalytic reaction is observed. Under similar conditions, the turnover number (kcat) of Se-4A4 is 42% of that of the natural rabbit liver cGPX. The Se-4A4 reaction involves a Ping Pong mechanism, which is the same as that of the natural cGPX. The selenocysteine residue is located in the binding site of the antibody and is shown to be crucial for this activity. Of the thiol compounds tested, only GSH is able to serve as substrate for Se-4A4. It was demonstrated, using the free-radical-damage system (hypoxanthine/xanthine oxidase) of cardiac mitochondria, that Se-4A4 can protect mitochondria from free-radical damage at least 10(4)-fold more effectively than the natural cGPX.
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