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Detailed particle-image velocimetry (PIV) measurements of flow fields inside semi-open impellers have been performed to understand better the internal flow patterns that are responsible for the unique performance of these centrifugal pumps operated in the range of very low specific speed. Two impellers, one equipped with six radial blades (impeller A) and the other with four conventional backward-swept blades (impeller B), are tested in a centrifugal pump designed to be operated at a non-dimensional specific speed of n s=0.24. Complex flow patterns captured by PIV are discussed in conjunction with the overall pump performance measured separately. It is revealed that impeller A achieves higher effective head than impeller B even though the flow patterns in impeller A are more complex, exhibiting secondary flows and reverse flows in the impeller passage. It is shown that both the localized strong outward flow at the pressure side of each blade outlet and the strong outward through-flow along the suction side of each blade are responsible for the better head performance of impeller A.

J. Kurokawa, H. Abriel and R. S. Kass. Molecular Basis of the Delayed Rectifier Current IKsin Heart. Journal of Molecular and Cellular Cardiology(2001) 33, 873–882. Electrical activity underlies the control of the frequency, strength, and duration of contraction of the heart. During the cardiac cycle, a regular rhythmic pattern must be established in time-dependent changes in ionic conductances in order to ensure events that underlie normal cardiac function. This pattern must be tightly regulated by sympathetic nervous activity to ensure a physiologically relevant relationship between diastolic filling and ejection times with variable heart rate. The duration of the ventricular action potential is controlled in part by a slowly activated potassium channel current, IKs. The molecular identity of the subunits that comprise the channels conducting this current is important, not only for understanding the fundamental mechanisms that control electrical activity in healthy individuals, but also for understanding the molecular basis of at least one inherited human disease, LQTS-1. This brief review summarizes key points of information regarding the molecular determinants of the activity of these channels, their relationship to human disease, and what is known, and yet to be discovered, about the molecular determinants of the regulation of this channel by sympathetic nervous activity.

The mechanism for the damage to the alanine-preferring amino acid transport system (A system) of guinea pig intestinal brush border membrane vesicles induced by active oxygen species was studied in vitro. The transport activity of L-proline, which is a model amino acid for the A system, and the tryptophan fluorescence intensity of intestinal brush border membrane vesicles were decreased, and lipid peroxidation of these membrane vesicles was induced by ultraviolet irradiation, which generated active oxygen species. Thiourea (hydroxyl radical scavenger) protected L-proline transport activity and tryptophan fluorescence intensity of intestinal brush border membrane vesicles and also inhibited lipid peroxidation in these membrane vesicles in the presence of active oxygen radicals. a-Tocopherol (singlet oxygen radical scavenger) inhibited lipid peroxidation of intestinal brush border membrane vesicles but protected neither L-proline transport activity nor trytophan fluorescence intensity in these membrane vesicles in the presence of active oxygen radicals. Catalase and superoxide dismutase showed no protective effect on L-proline transport activity, tryptophan fluorescence intensity, or lipid peroxide formation in intestinal brush border membrane vesicles in the presence of active oxygen radicals. These results suggest that the hydroxyl radicals play an important role in the damage to intestinal amino acid transport activity induced by active oxygen species and that this damage induced by hydroxyl radicals can be attributed to lipid peroxidation and decomposition of aromatic amino acids of membrane protein in intestinal brush border membrane vesicles.