Structure and function in the excretory systems of some terrestrial prosobranch snails (Cyclophoridae)

The excretory systems of terrestrial prosobranch snails of the family Cyclophoridae, collected in Jamaica, Costa Rica and South Africa, have been examined physiologically and as regards their gross and fine structure. The process of urine formation commences in the heart, where fluid is filtered across the wall of the ventricle. Filtration through the auricular wall is believed to be negligible. The kidney, which contains three types of cell, modifies the composition of the filtrate. One type of resorptive cell, characterized by basal infoldings associated with mitochondria, takes up salts. Another type, with basal subcellular spaces, may be responsible for taking up water. The third type of cell is secretory, producing concretions of uric acid and phospholipid which are liberated into the kidney lumen when the cell degenerates.
The rate and mechanism of urine production have been investigated using injections of inulin. The filtration rate at 25°C is 0.5 μl/g/min, and in 100% R.H. the average rate of urine production is 0–39 μl/g/min.
An accessory excretory organ has been developed from the hypobranchial gland of aquatic forms. It is composed of groups of subepithelial tubular glands opening into the mantle cavity by one or a series of pores, and secreting purines, phospholipids and mucus. There is evidence that this organ becomes progressively more complex in forms occupying drier habitats.
The systems of excretion and osmoregulation in the Cyclophoridae are considered to be very similar to those in their aquatic relatives, the Viviparidae and Ampullariidae. Certainly the cyclophorids are not as well adapted to a terrestrial life as are the Pulmonata, and in many respects they may be considered "aquatic" snails living on land.     

Monoamine transport in theOctopus posterior salivary gland nerves

Summary Noradrenaline (NA) and 5-hydroxytryptamine (5-HT) accumulated on the proximal side of a ligature to the posterior salivary gland (PSG) nerves in the octopus PSG duct. The NA concentration continued to increase proximally up to 18 days after ligation when a level of 59 g/g was reached compared with 12 g/g distally and 16–18 g/g for the corresponding portions of the normal duct. The concentration of 5-HT after the same period was 8.5 g/g proximally and 0.7 g/g distally compared to 4–7 g/g for normal duct. Dopamine (DM) was undetectable either after ligation or in the non-ligated duct. Accumulations of dense-core synaptic vesicles were observed by electron microscopy in some of the axons on both sides of the ligature.The NA concentration in the gland shows a decrease 6–8 days post-ligation and by 16–18 days had fallen to 50% of the normal value. No change in the DM or 5-HT concentrations had occurred by this time. When the nerves had been ligated for 40 days the 5-HT level in the gland had also decreased but the DM concentration was comparable to control values. It is concluded that NA is the predominant aminergic neurotransmitter in the PSG nerves and that its transport from the brain to the gland is a continuous process.Ligating or cutting the PSG duct caused a decrease in diameter of the distal nerve bundles but many axons did not degenerate even after 40 days ligation. The continued existence of some of the axons may explain the slow depletion of monoamines from the gland. Morphological changes in the secretory cells of the glandular tubules were observed by light microscopy 40 days after interruption of the nerve supply. It is suggested that the PSG nerves are required for the maintenance of the glandular tubules.     

Affinity labelling of the binding site of rabbit antibody. Evidence for the involvement of the hypervariable regions of the heavy chain

The binding sites of rabbit antibodies with affinity for the haptenic group 4-azido-2-nitrophenyl-lysine have been specifically labelled by photolysis of the hapten-antibody complex. The extent of covalent labelling was 0.5-0.9mol of hapten bound/mol of antibody and, by using an immunoadsorbent, antibody with 1.3mol of hapten/mol was obtained. The antibody was specifically labelled in the binding site and the ratio of labelling of heavy and light chains was in the range 3.3-5.0. The labelled heavy chains were cleaved by CNBr treatment and after reduction and alkylation of the intrachain bonds, were digested with trypsin. Evidence is presented that two regions of the heavy chain, positions 29-34 and 95-114, together contain about 80% of the label on the heavy chain; these two regions respectively include two of the hypervariable regions of rabbit heavy chain.     

Effect of Lytic Enzymes of Acanthamoeba castellanii on Bacterial Cell Walls

Extracts of Acanthamoeba castellanii (Neff) contain alpha- and beta-glucosidase, beta-galactosidase, beta-N-acetylglucosaminidase, amylase, and peptidase. All of these activities are optimal between pH 3 and 4. These extracts also were found to clarify suspensions of cell walls from nine different gram-positive bacteria, including Micrococcus lysodeikticus. The pH optimum for the lytic activity was between 3 and 4. The extent of lysis of the various cell walls did not correlate with the release of free amino groups and of free N-acetylated sugars from the walls during digestion with these extracts. Suspensions of cell walls of Escherichia coli (a gram-negative bacterium), Cordiceps militaris (a fungus), and Acanthamoeba cysts, as well as of colloidal chitin, were not clarified by incubation with these extracts, although reducing sugars were released from each of these materials. Exhaustive digestion of M. lysodeikticus walls by lysozyme released no free N-acetylglucosamine. The products of exhaustive digestion of this cell wall with Acanthamoeba extracts were free N-acetylglucosamine, free N-acetylmuramic acid, glycine, alanine, glutamic acid, lysine, and N-acetylmuramic acid peptide fragments. These results suggest that the amoeba extracts contain endo- and exo-hexosaminidases, in addition to beta-hexosaminidase and peptide hydrolases.     

The Contractile and Control Sites of Natural Actomyosin

The various contractile and control sites of natural actomyosin gel were studied by comparing the kinetics of ATP hydrolysis with those of gel contraction, measured as an increase in turbidity. Contraction of actomyosin gel seems to require the cooperative reaction of ATP (with Mg) at two different sites. One of these sites catalyzes the hydrolysis of ATP and most probably contributes the driving force for contraction; the binding of ATP to the other site appears to break certain links that retard movement of the gel components. At limiting concentrations of ATP, the rate of contraction seems to depend on the rate of breaking these links as well as on the rate of ATP hydrolysis. But when both sites are saturated, the rate of contraction appears to be limited only by the rate of ATP hydrolysis. In addition to these two contractile sites, there are also two different control sites. At one, the relaxing site, the binding of ATP with Mg inhibits ATP hydrolysis and gel contraction. At the other, the binding of calcium activates contraction by overcoming the inhibitory action of Mg and ATP at the relaxing site. This control system—inhibition by substrate and disinhibition by calcium—can be selectively inactivated by heat and reactivated by dithiothreitol, a disulfide-reducing agent. These observations on the isolated contractile system are discussed in relation to the contraction and relaxation of muscle.     

Protein synthesis by microsomal particles from regenerating rat liver

1. Washed microsome particles from regenerating liver were shown to incorporate [(14)C]leucine into protein more actively than similar preparations from normal liver. 2. The total incorporation in the preparations from regenerating liver increased linearly with the amount of protein incubated, whereas this was not so with preparations from normal liver. 3. The greater activity of regenerating-liver microsomes appeared to be associated with the bound polysomes. 4. The size distribution of polysomes obtained after removal of membrane with deoxycholate was the same in normal and regenerating liver. 5. In general the activity of polysome preparations from normal and regenerating liver was similar. 6. It is concluded that the greater activity of the particles in the microsome fraction from regenerating liver is to be attributed to the ribosomes bound to membrane and that their activity is controlled by factors present in the membrane.     

Effect of exogenous serum gonadotrophin (PMS) on aspects of reproductive development in female domesticated canaries

PMS was injected thrice weekly for four weeks into first winter and second winter canaries during the following periods: September-October, November-December, January-February and February-March. Measures were made of ovary and oviduct weight, brood-patch development (defeathering, vascularity and sensitivity changes), nest-building and egg-laying. PMS caused overy growth in all months: this was greatest in the second year birds in February. Both control and treated ovaries increased in size towards the breeding season. Oviduct growth depends mainly on the size of the treated ovary. Defeathering was produced by PMS in all months: its rate and extent increased towards the breeding season. Vascularity was also produced by PMS. It was least in November-December but after that the rate at which it appeared increased towards the breeding season. By contrast, the effect of PMS on brood-patch skin sensitivity was greater in the autumn group than subsequently. Nest-building occurred in September-October, but was then very slight until February-March, which is the beginning of the breeding season. Eggs were laid in most months; fewer injections were needed to produce egg-laying as the breeding season approached.