Stable isotope evidence of food web connectivity by a top predatory fish ( Argyrosomus japonicus

In this study, food web connectivity within the Kowie Estuary on the south-east coast of South Africa was evidenced by the trophic behaviour of the predominantly piscivorous Argyrosomus japonicus. We examined stable isotopes of carbon (δ13C) and nitrogen (δ15N) in the dominant consumers (zooplankton, invertebrates and fishes) and food sources (particulate organic matter, epibionts and benthic microalgae) in the system. An SIAR (Stable Isotope Analysis in R) mixing model was used to interpret the possible food sources for this dominant top predatory fish. Small fishes and large epibenthic invertebrates dominated the diet of A. japonicus. Based on the contrasting diet of these prey fish and invertebrates, we propose that organic matter enters the predatory fish community via two major pathways: (1) a littoral pathway dominated by benthic microalgae production and epibionts, and (2) a channel pathway dominated by suspended particulate organic matter (including phytoplankton). We conclude that the highly mobile A. japonicus consumes both pelagic and benthic fauna from the littoral and channel zones of the estuary, thereby playing a key functional role in linking food webs. This dietary diversity may help explain the success of A. japonicus as a dominant top predator in the system, primarily by increasing the energy available to this species

Modulation By K+ Plus NH4+ of Microsomal (Na+, K+)-ATPase Activity in Selected Ontogenetic Stages of the Diadromous River Shrimp Macrobrachium amazonicum (Decapoda, Palaemonidae)

We investigate the synergistic stimulation by K(+) plus NH(4) (+) of (Na(+), K(+))-ATPase activity in microsomal preparations of whole zoea I and decapodid III, and in juvenile and adult river shrimp gills. Modulation of (Na(+), K(+))-ATPase activity is ontogenetic stage-specific, and particularly distinct between juveniles and adults. Although both gill enzymes exhibit two different sites for K(+) and NH(4) (+) binding, in the juvenile enzyme, these two sites are equivalent: binding by both ions results in slightly stimulated activity compared to that of a single ionic species. In the adult enzyme, the sites are not equivalent: when one ion occupies its specific binding site, (Na(+), K(+))-ATPase activity is stimulated synergistically by ≈50% on binding of the complementary ion. Immunolocalization reveals the enzyme to be distributed predominantly throughout the intralamellar septum in the gill lamellae of juveniles and adults. Western blot analyses demonstrate a single immunoreactive band, suggesting a single (Na(+), K(+))-ATPase α-subunit isoform that is distributed into different density membrane fractions, independently of ontogenetic stage. We propose a model for the modulation by K(+) and NH(4) (+) of gill (Na(+), K(+))-ATPase activity. These findings suggest that the gill enzyme may be regulated by NH(4) (+) during ontogenetic development in M. amazonicum