Is the emergency ambulance service abused?

Analysis of 1000 consecutive patients brought to the accident and emergency department of a busy district general hospital by ambulance after emergency "999" telephone calls showed that 51.7% of these journeys were unnecessary. Medical cases accounted for a greater percentage of necessary calls than did trauma and surgical cases. Medical education of the public is essential if the number of these calls is to be cut.     

The association of FAD with the cytochrome b−245 of human neutrophils

A plasma membrane fraction prepared from human neutrophils had a fluorescence resembling that of a fluorescent flavoprotein, with emission maximum near 520nm and excitation maxima near 380 and 460nm. The fluorescence emission and excitation properties of Triton N-101-solubilized membrane fraction resembled those of FAD. FAD was present in the membranes at a concentration of 417pmol/mg of protein and cytochrome b₋₂₄₅ at a concentration of 407pmol/mg of protein. In a 110-fold purified preparation of cytochrome b₋₂₄₅ the ratio of FAD:cytochrome b was 1:1. Analytical gradient centrifugation of neutrophil homogenates shows a coincidence of two cytochrome b peaks and two peaks of fluorescence, corresponding with plasma membrane and specific granule fractions; most of the FAD was non-fluorescent and located in fractions lighter than the plasma membrane. Plasma membrane fractions prepared from neutrophils of patients suffering from the X-linked form of chronic granulomatous disease lacked cytochrome b and contained 194pmol of FAD/mg of protein; plasma membrane fractions prepared from neutrophils of patients with the autosomal recessive form of chronic granulomatous disease contained both cytochrome b₋₂₄₅ and FAD in the normal range of concentrations in a ratio of 1:1. Phagocytic vesicles were prepared from normal neutrophils and found to contain FAD and cytochrome b in a ratio 2.22:1, suggesting that activation of neutrophils many involve the incorporation of an additional flavin into the membrane. Under anaerobic conditions in the presence of EDTA to act as an electron donor to a flavin, the cytochrome b₋₂₄₅ of neutrophil membranes was partly (12%) photoreducible, an effect increased to 100% by the addition of FMN. The extent of reduction of cytochrome b in an anaerobic neutrophil homogenate containing NADH increased from 30% to 70% on illumination. We suggest that these results indicate a close association between FAD and cytochrome b₋₂₄₅ and support a scheme for electron transport thus: [Formula: see text]     

Ablation of PLB exacerbates ischemic injury to a lesser extent in female than male mice: protective role of NO

Recent studies suggest a role for phospholamban phosphorylation during ischemia and reperfusion. The role of phospholamban in ischemia was studied by subjecting hearts from male and female wild-type (MWT/FWT) and phospholamban-knockout (MKO/FKO) mice to 20 min of ischemia-40 min of reperfusion while (31)P NMR spectra were acquired. ATP and pH values fell lower during ischemia, and postischemic contractility was less, in MKO and FKO versus WT hearts. After shorter ischemia (15 min), recoveries of contraction, ATP, and pH were greater in FKO than MKO hearts. To examine the role of nitric oxide (NO) synthases (NOS) in the protection in FKO versus MKO hearts, we utilized 1 microM l-NAME, a NOS inhibitor, or 100 microM S-nitroso-N-acetylpenicillamine (SNAP), an NO donor. Recoveries of function, ATP, and pH were less in l-NAME-treated FKO than untreated FKO hearts and greater in SNAP-treated MKO than untreated MKO hearts. In conclusion, phospholamban ablation increased ischemic injury in both males and females; however, female hearts were less susceptible than male hearts. Protection in females was decreased by a NOS inhibitor and mimicked in males by an NO donor, implying that protection was NOS mediated.     

Collection and culture techniques for gelatinous zooplankton

Gelatinous zooplankton are the least understood of all planktonic animal groups. This is partly due to their fragility, which typically precludes the capture of intact specimens with nets or trawls. Specialized tools and techniques have been developed that allow researchers and aquarists to collect intact gelatinous animals at sea and to maintain many of these alive in the laboratory. This paper summarizes the scientific literature on the capture, collection, and culture of gelatinous zooplankton and incorporates many unpublished methods developed at the Monterey Bay Aquarium in the past 15 years.     

Protein profiled features patterned via confocal microscopy

Protein patterns were printed using conventional microlithographic materials in a bilayer arrangement and unconventional exposure tools. The bilayer resist stack consisted of a lower poly(tert-butyl methacrylate) layer and an upper diazonaphtoquinone/novolak layer. The protein features were printed in either 'contact printing', or 'step and repeat' mode. The latter printing mode can be managed in a flow-cell consisting of a standard microscope slide and cover slip, spaced apart by about 20 microm, as follows: (i) the exposure step is carried out in the cell using focused 488 nm beam of a confocal laser scanning microscope; (ii) the development step is performed by flowing the photoresist developer through the cell; (iii) the selective deposition of the protein (FITC-labelled avidin) is achieved via the flow of the protein solution through the cell until a desired contrast has been reached; (iv) the control of the process is assured using on-line monitoring of the photo-activated red fluorescence of the developing resist layer, and of the green fluorescence of the FITC-protein patterns, respectively. The protein printing technique uses equipment routinely available in biological laboratory. The 'step and repeat' patterning yields high and controllable resolution. The process can be applied in the fabrication of medical microanalysis devices.