Energy requirements of beavers (Castor canadensis) swimming underwater.

Energy requirements of beavers (Castor canadensis) swimming voluntarily underwater were investigated in Neumünster Zoo (Germany) in a covered, still-water swim channel with oxygen and carbon dioxide respirometry. During the experiments, all activities of the beavers were monitored and recorded. While at rest within their thermoneutral zone on land (17 degrees C), beavers had a respiratory quotient of 0.95 and a resting metabolic rate of 1.58 W kg-1. When resting in water, energy requirements rose to 2.31 W kg-1. When swimming underwater in the channel, beavers preferred a mean speed of 0.64 m s-1, and their energy requirements rose to 2.64 W kg-1. Cost of transport, however, was minimal at 0.9 m s-1 and amounted to 0.36 J N-1 m-1. Although beavers must compromise form and function to operate on water and on land, their energy requirements while diving amount to only 1.65 times the resting metabolic rate and compare well with those of accomplished swimmers such as aquatic mammals and birds.

Diving energetics in king penguins (Aptenodytes patagonicus).

Dive duration in wild king penguins and the energetic cost of swimming in a 30m long swim channel were determined at Ile de la Possession, Crozet Archipelago, using external data loggers and respirometry, respectively. Calibrated electronic data loggers equipped with a pressure sensor were used to determine dive durations: 95% of dives were less than 6 min long and 66% of dives were less than 4 min long. Dive patterns show that king penguins may intersperse long dive durations (4-6.3 min) with short ones (1.5-3 min) and make surface pauses of variable duration between them (0.5-3.5 min), or dive regularly (for up to 5 h) with long dive durations (5 min) and constant interdive surface intervals (1.5 min). The latter indicates that the aerobic dive limits (ADL) of this species could be higher and oxygen consumption lower than previously reported. Assuming that king penguins dive within their aerobic limit, different approaches to the analysis of the data obtained in the swim channel are discussed to derive the ADL. Swimming speeds observed in the channel ranged from 0.9 to 3.4 m s-1. Transport costs were lowest between 1.8 and 2.2 m s-1. Although at 2.2 m s-1 king penguins used only 10.3 Wkg-1 over a dive+surface cycle (minimal transport costs of 4.7 J kg-1 m-1), we speculate that tisse oxygen consumption during submergence may be as low as 0.23 ml O2 kg-1 s-1 (2.1 times standard metabolic rate, SMR) or perhaps lower (which gives an ADL of 4.2 min). During surface phases, oxygen uptake would be increased to at least 1 ml O2kg-1 s-1 (9.3 times SMR). This implies that at least 70% of all dives are aerobic. Potential physiological mechanisms allowing king penguins to partition O2 consumption between submergence and surface periods remain, however, unclear.

Effect of fat feeding on intestinal alkaline phosphatase activity in tissue and serum.

Serum intestinal alkaline phosphatase activity is increased by fat feeding, but the mechanism of this increase is not fully understood. Fasting rats were fed a single feed of either corn oil (12 kcal) or an isocaloric elemental feed (Vivonex 100 HN). Changes in enzyme activity in the small bowel mucosa and serum were followed for 20 h. Only the fat-fed rats had increased serum enzyme activity, being maximal at 7 h and three times the fasting level. This resulted from an increase in the amount of enzyme protein in the serum and not from an increase in its catalytic efficiency. The serum biological half-life of 125I-labeled intestinal alkaline phosphatase was the same in fasted (2.51 min) and fat-fed rats (2.55 min). Both types of feed caused a quantitatively similar increase in brush-border-bound alkaline phosphatase activity. However, levels of soluble intracellular alkaline phosphatase in intestinal mucosa were affected differently: the elemental diet caused a substantial rise, whereas no significant change was seen after fat feeding. The isoelectric pattern of phosphatase activity in serum after fat feeding was identical to that of soluble intracellular and not membranous alkaline phosphatase. Therefore, serum intestinal alkaline phosphatase activity rises in response to a single fat feed as a result of increased delivery of the enzyme to the blood and not as a result of an increase in its normally short biological half-life. This rise cannot be directly linked to an increase in the amount of brush-border-bound enzyme, and it appears that the serum enzyme is derived directly from a pool of soluble intracellular enzyme in the small bowel mucosa.