The input of terrestrial invertebrates from tree canopies to a stream

SUMMARY. The input of terrestrial invertebrates from different tree canopies to a trout stream was determined for a 28-week period from April to October, 1980. Sycamore produced the greatest number of animals, followed by oak and alder. Ash was not significantly different from the controls. Coleoptera, Diptera, Homoptera and Arachnida made up the greatest number of animals caught, with Lepidoptera larvae important beneath oak. The input of biomass (g m^-2 dry wt) was also greatest beneath sycamore (35.80), followed by oak (27.76), alder (20.39), ash (11.15) and control (9.92). The input of biomass was bimodal. The significance of terrestrial invertebrates as food for salmonids is discussed.     

Group-selective reagent modification of the sodium- and chloride-coupled glycine transporter under native and reconstituted conditions.

Glycine transporter from rat brain stem and spinal cord is inactivated by specific sulfhydryl reagents. Modification of lysine residues also promotes a decrease of the transporter activity but in a lesser extent than that promoted by thiol group reagents. Mercurials showed a more marked inhibitory effect than maleimide derivatives. SH groups display a similar reactivity for p-chloromercuribenzenesulfonate (pCMBS) and mersalyl in synaptosomal membrane vesicles and proteoliposomes reconstituted with the solubilized transporter. However, different reactivity is observed with N-ethylmaleimide (MalNEt), the greatest effect being attained in membrane vesicles. The rate of inactivation by pCMBS and MalNEt is pseudo-first-order showing time- and concentration-dependence. pCMBS and MalNEt decrease the Vmax for glycine transport and to a lesser extent act on the apparent Km. Treatment with dithiothreitol (DTT) of the transporter modified by pCMBS results in a complete restoration of transporter activity indicating that the effect exercised by the reagent is specific for cysteine residues on the protein. It is concluded that SH groups are involved in the glycine transporter function and that these critical residues are mostly located in a relatively hydrophilic environment of the protein.