Temperature-Dependent Swimming Performance Differs by Species: Implications for Condition-Specific Competition between Stream Salmonids

2020 ◽  
Vol 37 (5) ◽  
pp. 1 ◽  
Author(s):  
Taihei Yamada ◽  
Itsuro Koizumi ◽  
Hirokazu Urabe ◽  
Futoshi Nakamura
Keyword(s):  
Swimming Performance ◽  
Temperature Dependent ◽  
Stream Salmonids

scholarly journals STUDIES OF TROPICAL TUNA SWIMMING PERFORMANCE IN A LARGE WATER TUNNEL - ENERGETICS

1994 ◽  
Vol 192 (1) ◽  
pp. 13-31 ◽  
Author(s):  
H Dewar ◽  
J Graham
Keyword(s):  
Swimming Performance ◽  
Standard Metabolic Rate ◽  
Water Tunnel ◽  
Scaling Exponent ◽  
Temperature Dependent ◽  
Katsuwonus Pelamis ◽  
Size Groups ◽  
Large Water ◽  
Euthynnus Affinis ◽  
Tropical Tuna

The metabolic rates (V(dot)O2) of three tropical tunas [yellowfin tuna (Thunnus albacares), kawakawa (Euthynnus affinis) and skipjack (Katsuwonus pelamis)] were estimated using a large water-tunnel respirometer. Experiments lasting up to 31 h were used to determine the effects of velocity (U) on tuna V(dot)O2 over a range of U (17-150 cm s-1) and temperatures (18­30°C). Replicate tests were carried out on several fish. The swimming V(dot)O2 of yellowfin is temperature-dependent (Q10=1.67, determined over intervals of 3­5°C). For yellowfin and skipjack, it was also possible to partition metabolic costs between maintenance and locomotion. The standard metabolic rate (SV(dot)O2) was estimated by extrapolation of the U/V(dot)O2 function to U=0. Comparisons of SV(dot)O2 for different size groups of yellowfin show that the mass-specific scaling exponent for V(dot)O2 is -0.40. The SV(dot)O2 of tuna is comparable to values determined previously by stasis respirometry and is approximately three times higher than that of salmonids. Further comparisons with salmonids show that the slope of the U/V(dot)O2 function is less for tunas, which demonstrate a greater swimming efficiency.

scholarly journals Interacting Effects of Cell Size and Temperature on Gene Expression, Growth, Development and Swimming Performance in Larval Zebrafish

2021 ◽  
Vol 12 ◽  
Author(s):  
Iris Louise Eleonora van de Pol ◽  
Adam Hermaniuk ◽  
Wilhelmus Cornelis Egbertus Petrus Verberk
Keyword(s):  
Gene Expression ◽  
Cell Size ◽  
Citrate Synthase ◽  
Swimming Performance ◽  
Interactive Effects ◽  
Temperature Dependent ◽  
Thermal Biology ◽  
Expression Of Genes ◽  
Different Temperatures ◽  
Growth Development

Cell size may be important in understanding the thermal biology of ectotherms, as the regulation and consequences of cell size appear to be temperature dependent. Using a recently developed model system of triploid zebrafish (which have around 1.5-fold larger cells than their diploid counterparts) we examine the effects of cell size on gene expression, growth, development and swimming performance in zebrafish larvae at different temperatures. Both temperature and ploidy affected the expression of genes related to metabolic processes (citrate synthase and lactate dehydrogenase), growth and swimming performance. Temperature also increased development rate, but there was no effect of ploidy level. We did find interactive effects between ploidy and temperature for gene expression, body size and swimming performance, confirming that the consequences of cell size are temperature dependent. Triploids with larger cells performed best at cool conditions, while diploids performed better at warmer conditions. These results suggest different selection pressures on ectotherms and their cell size in cold and warm habitats.

The Effect of Temperature on the Burst Swimming Performance of Fish Larvae

1992 ◽  
Vol 170 (1) ◽  
pp. 187-201 ◽  
Author(s):  
R. S. BATTY ◽  
J. H. S. BLAXTER
Keyword(s):  
High Speed ◽  
Stride Length ◽  
Fish Larvae ◽  
Swimming Performance ◽  
Beat Frequency ◽  
Effect Of Temperature ◽  
Temperature Dependent ◽  
Burst Swimming ◽  
Tail Beat ◽  
Escape Speed

Newly hatched herring and plaice larvae were stimulated by probes to make C-start escape responses at temperatures between 5 and 15 °C. The responses and the subsequent burst-speed swimming were recorded and analysed using high-speed video at 400 frames s−1. The muscle contraction time of the initial C-start was temperature-dependent, ranging from 22–33 ms at 5°C to 17–21 ms at 15°C. Immediately following the C-start, tail-beat frequency ranged from 18s−1 at 5°C to 35 s−1 at 15°C. Tail-beat amplitude, equivalent to 0.4-0.6 of a body length (L), and stride length, about 0.5 L, were not temperature-dependent. The escape speed ranged from 8 Ls−1 at 5°C to 15 Ls−1 at 15 °C. These results and those of other workers can be described by the equation: f=100e−99/(t+29.5)L−0.266, where f is tail-beat frequency, t is temperature and L is length.

(111) Monocrystalline Nickel Films

1972 ◽  
Vol 30 ◽  
pp. 512-513
Author(s):  
T.E. Pratt ◽  
R.W. Vook
Keyword(s):  
Film Thickness ◽  
Deposition Rate ◽  
Room Temperature ◽  
Narrow Range ◽  
High Vacuum ◽  
Residual Pressure ◽  
Temperature Dependent ◽  
Deposition Parameters ◽  
Transmission Electron ◽  
Substrate Temperatures

(111) oriented thin monocrystalline Ni films have been prepared by vacuum evaporation and examined by transmission electron microscopy and electron diffraction. In high vacuum, at room temperature, a layer of NaCl was first evaporated onto a freshly air-cleaved muscovite substrate clamped to a copper block with attached heater and thermocouple. Then, at various substrate temperatures, with other parameters held within a narrow range, Ni was evaporated from a tungsten filament. It had been shown previously that similar procedures would yield monocrystalline films of CU, Ag, and Au.For the films examined with respect to temperature dependent effects, typical deposition parameters were: Ni film thickness, 500-800 A; Ni deposition rate, 10 A/sec.; residual pressure, 10-6 torr; NaCl film thickness, 250 A; and NaCl deposition rate, 10 A/sec. Some additional evaporations involved higher deposition rates and lower film thicknesses.Monocrystalline films were obtained with substrate temperatures above 500° C. Below 450° C, the films were polycrystalline with a strong (111) preferred orientation.

In Vitro Effects of Urokinase — Prevention by Different Inhibitors

1990 ◽  
Vol 64 (03) ◽  
pp. 402-406 ◽  
Author(s):  
M D Oethinger ◽  
E Seifried
Keyword(s):  
In Vitro Study ◽  
Thrombin Time ◽  
Plasma Samples ◽  
Temperature Dependent ◽  
Chloromethyl Ketone ◽  
Control Value ◽  
Dose Time ◽  
In Vitro Effects ◽  
Full Protection

SummaryThe present in vitro study investigated dose-, time- and temperature-dependent effects of two-chain urokinase plasminogen activato(u-PA, urokinase) on normal citrated plasma. When 10 μg/ml u-PA wereadded to pooled normal plasma and incubated for 30 min at an ambient temperature (25° C), α2-antiplas-min decreased to 8% of the control value. Incubation on ice yielded a decrease to 45% of control,whereas α2-antiplasmin was fully consumed at 37° C. Fibrinogen and plasminogen fell to 46% and 39%, respectively, after a 30 min incubation at 25° C. Thrombin time prolonged to 190% of control.Various inhibitors were studied with respect to their suitability and efficacy to prevent these in vitro effects. Aprotinin exhibited a good protective effect on fibrinogen at concentrations exceeding 500 KlU/ml plasma. Its use, however, was limited due to interferences with some haemostatic assays. We could demonstrate that L-Glutamyl-L-Glycyl-L-Arginyl chloromethyl ketone (GGACK) and a specific polyclonal anti-u-PA-antibody (anti-u-PA-IgG) effectively inhibited urokinase-induced plasmin generation without interfering with haemostatic assays. The anti-u-PA-antibody afforded full protection ofα2-antiplasmin at therapeutic levels of u-PA.It is concluded that u-PA in plasma samples from patients during thrombolytic therapy may induce in vitro effects which should be prevented by the use of a suitable inhibitor such as GGACK or specific anti-u-PA-antibody.

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