Morning flight behavior of nocturnally migrating birds along the western basin of Lake Erie

Many species of birds that normally migrate during the night have been observed engaging in so‐called morning flights during the early morning. The results of previous studies have supported the hypothesis that one function of morning flights is to compensate for wind drift that birds experienced during the night. Our objective was to further explore this hypothesis in a unique geographic context. We determined the orientation of morning flights along the southern shore of Lake Erie's western basin during the spring migrations of 2016 and 2017. This orientation was then compared to the observed orientation of nocturnal migration. Additionally, the orientation of the birds engaged in morning flights following nights with drifting winds was compared to that of birds following nights with non‐drifting winds. The morning flights of most birds at our observation site were oriented to the west‐northwest, following the southern coast of Lake Erie. Given that nocturnal migration was oriented generally east of north, the orientation of morning flight necessarily reflected compensation for accumulated, seasonal wind drift resulting from prevailingly westerly winds. However, the orientation of morning flights was similar following nights with drifting and non‐drifting winds, suggesting that birds on any given morning were not necessarily re‐orienting as an immediate response to drift that occurred the previous night. Given the topographical characteristics of our observation area, the west‐northwest movement of birds in our study is likely best explained as a more complex interaction that could include some combination of compensation for wind drift, a search for suitable stopover habitat, flying in a direction that minimizes any loss in progressing northward toward the migratory goal, and avoidance of a lake crossing.     

Scribed transparency microplates mounted on a modified standard microplate

The immense cost effectiveness of using transparencies as analyte handling implements in microplate instrumentation offers the possibility of application even in resource-limited laboratories. In this work, a standard microplate was adapted to serve as the permanent base for disposable scribed transparencies. The approach is shown to ameliorate evaporation, which can affect assay accuracy when analytes need to be incubated for some time. It also offers assurance against fluorescence measurement errors due to the cross-talk of samples from adjacent wells.     

Patch exploitation by small gadoids: evidence for an asymmetric tidal effect

The attraction of small gadoids to physically disturbed seabed patches was examined experimentally using a modified remote operated vehicle. Video observations were made of simulated disturbances to investigate the influence of tidal state, time of day and current speed on the pattern of exploitation. Fish were more likely to be present in disturbed patches, and when present, occurred in significantly greater numbers than in control areas. However, this response was dependent on tidal state, occurring only on rising tides.     

A medium for the isolation, enumeration and rapid presumptive identification of injured Clostridium perfringens and Bacillus cereus

A blood-free egg yolk medium (BCP) containing pyruvate, inositol, mannitol and a bromocresol purple indicator in a nutrient agar base has been developed to initiate the growth of Clostridium perfringens . It is comparable to blood agar for the growth of normal, chilled stored vegetative cells and heat-injured spores of Cl. perfringens and Bacillus cereus . It has the advantage over blood agar in exhibiting presumptive evidence of Cl. perfringens (production of lecithinase and inositol fermentation) after an overnight incubation at 43°C-45°C. Pyruvate, catalase and other hydrogen peroxide degraders were found to remove toxins rapidly formed in media exposed to air and light. Free radical scavengers of superoxide, hydroxyl ions and singlet oxygen were ineffective. Without scavengers the formation of 10–20 μg/ml hydrogen peroxide in the exposed medium was indicated and found lethal to injured Cl. perfringens .
The BCP medium has been used successfully for the rapid identification and enumeration of Cl. perfringens in foods and faeces from food poisoning outbreaks and cases of suspected infectious diarrhoea. Greater recovery of severely injured vegetative Cl. perfringens could be obtained by pre-incubation at 37°C of inoculated media for 2–4 h followed by overnight incubation at 43°C-45°C. Tryptose-sulphite-cyclo-serine and Shahidi-Ferguson-perfringens agar base were found to inhibit the growth of several strains of injured vegetative Cl. perfringens . This was not completely overcome by the addition of pyruvate. The inclusion of mannitol also allows the medium to be used for the presumptive identification of B. cereus . Growth and lecithinase activity are profuse on BCP. Heat-injured spores are recovered equally well on BCP and blood agar. A scheme for the identification of some other clos-tridia on BCP is presented.     

Depression after myocardial infarction.

The Minnesota Multiphasic Personality Inventory was completed by 101 patients 16 to 18 months after a proved myocardial infarction. The data suggested a bimodal distribution of patients. One class of patients had a relatively "normal" personality score apart from a tendency to hypomania. The second class had severe depression, with associated hysteria, hypochondriasis and psychasthenia. The severely depressed patients were older, with a greater tendency to hypertension and angina, and a tendency to smaller gains in aerobic power despite an equal intensity of endurance training. The distinction between "normal" and "depressed" postinfarction patients seems of some clinical importance, for the two classes of patients require opposite supportive techniques--restraint and encouragement, respectively.     

The measurement of 18-hydroxy-11-deoxycorticosterone in human plasma by radioimmunoassay

A radioimmunoassay method for the measurement of plasma levels of 18-hydroxy-11-deoxycorticosterone (18-OH-DOC) has been developed. The antiserum against 18-OH-DOC was produced in rabbits immunized against 18-OH-DOC-3-oxime-bovine serum albumin. Plasma (1–2 ml) was extracted with dichloromethane and chromatographed on paper. The purified extracts were incubated with antiserum at a $\text{1}\text{22,000}$ dilution for $\text{1}\text{2}$ hour at 37°C and for 2 hours at 4°C. Saturated ammonium sulfate was used to separate free from bound 18-OH-DOC. 1, 2-³H-18-OH-DOC was added to all samples to correct for losses and to determine the percent free. Pyridine (0.1%) was added to solvents to maintain the stability of 18-OH-DOC. Recovery after extraction was 58 ± 8 (S.D.)%. The accuracy and precision of the method were acceptable, and a sensitivity of 2 pg per sample enabled the measurement of very low levels of 18-OH-DOC. High specificity was demonstrated by a low blank value (0 ± 0.2 pg) and by demonstrating that alternative paper chromatography separation systems gave results not differing significantly from those obtained by the present method. The mean 8AM plasma 18-OH-DOC level was 8.5 ± 1.2 ng per 100 ml in 18 normotensive control subjects. There was a marked response of plasma 18-OH-DOC to ACTH stimulation and dexamethasone suppression and a significant increase after 3 hours upright posture.     

Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochrome c

Two forms of cytochrome c-specific methyltransferases from Euglena gracilis were purified approximately 100- and 50-fold, respectively, using DEAE-cellulose and gel-filtration chromatography. The methylation product of enzyme I was identified as S-methylmethionine and that of enzyme II as NG-monomethylarginine. Both enzymes were located in the cytosol and exhibit maximum activity at pH 7.0. Among the various proteins tested as substrates, the enzymes were highly specific toward cytochrome c. Various types of histones, in particular, were not modified by either enzyme. The molecular weights of enzyme I and II were 28,000 and 36,000, respectively. Various S-adenosyl-L-homocysteine analogs were tested for their inhibitory activity toward the enzymes. Only the D- and L-isomers of S-adenosylhomocysteine and sinefungin were significantly inhibitory. The Ki values for S-adenosyl-L-homocysteine were 8.13 X 10(-6) and 1.17 X 10(-5) M for enzyme I and II, respectively. Two-dimensional peptide mapping revealed the methylation site of enzyme I to be the methionine residue at position 65 while that of enzyme II to be the arginine residue at position 38. The methylation of either methionine or arginine residues by enzyme I and II, respectively, lowers the isoelectric point (pI) of cytochrome c: 9.23, 9.33, and 10.06 for S-methylmethionine-, NG-monomethylarginine-modified, and unmodified cytochrome c, respectively.     

A recombinant multimeric immunoglobulin expressed in rice shows assembly-dependent subcellular localization in endosperm cells

To investigate the role of subunit assembly in the intracellular deposition of multimeric recombinant proteins, we expressed a partially humanized secretory immunoglobulin in rice endosperm cells and determined the subcellular locations of the assembled protein and its individual components. Transgenic rice plants expressing either individual subunits or all the subunits of the antibody were generated by particle bombardment, and protein localization was determined by immunoelectron microscopy. Assembly of the antibody was confirmed by immunoassay and coimmunoprecipitation. Immunolocalization experiments showed no evidence for secretion of the antibody or any of its components to the apoplast. Rather, the nonassembled light chain, heavy chain and secretory component accumulated predominantly within endoplasmic reticulum-derived protein bodies, while the assembled antibody, with antigen-binding function, accumulated specifically in protein storage vacuoles. These results show that the destination of a complex recombinant protein within the plant cell is influenced by its state of assembly.