Recovery of indium from LCD screens of discarded cell phones.

Advances in technological development have resulted in high consumption of electrical and electronic equipment (EEE), amongst which are cell phones, which have LCD (liquid crystal display) screens as one of their main components. These multilayer screens are composed of different materials, some with high added value, as in the case of the indium present in the form of indium tin oxide (ITO, or tin-doped indium oxide). Indium is a precious metal with relatively limited natural reserves (Dodbida et al., 2012), so it can be profitable to recover it from discarded LCD screens. The objective of this study was to develop a complete process for recovering indium from LCD screens. Firstly, the screens were manually removed from cell phones. In the next step, a pretreatment was developed for removal of the polarizing film from the glass of the LCD panels, because the adherence of this film to the glass complicated the comminution process. The choice of mill was based on tests using different equipment (knife mill, hammer mill, and ball mill) to disintegrate the LCD screens, either before or after removal of the polarizing film. In the leaching process, it was possible to extract 96.4 wt.% of the indium under the following conditions: 1.0M H2SO4, 1:50 solid/liquid ratio, 90°C, 1h, and stirring at 500 rpm. The results showed that the best experimental conditions enabled extraction of 613 mg of indium/kg of LCD powder. Finally, precipitation of the indium with NH4OH was tested at different pH values, and 99.8 wt.% precipitation was achieved at pH 7.4.

Partial purification of plasma phenoloxidase of the yellow fever mosquito Aedes aegypti L. (Diptera: Culicidae).

A nitrocellulose-based assay was developed using a dot-blot apparatus to detect phenoloxidase activity in column fractions. Using this assay, plasma phenoloxidase was partially purified from Aedes aegypti larvae using hydrophobic interaction chromatography, gel filtration, and ion-exchange chromatography. The molecular weight (M(r)) native enzyme was 130,000, and it contained subunits of 76,000, 62,000, and 58,000. Two phenoloxidase peaks were observed by ion exchange chromatography, and these fractions had distinct polypeptide profiles as detected by SDS-PAGE.

Mosquito DNA polymerase epsilon.

The mosquito homolog of mammalian DNA polymerase epsilon, formerly known as a proliferating cell nuclear antigen (PCNA)-independent form of DNA polymerase delta, has been purified from mosquito larval extracts. The polymerase epsilon was separated from DNA polymerase alpha by chromatography on hydroxylapatite, and the enzyme was subsequently purified on single-stranded DNA agarose, followed by a 5' AMP-agarose chromatography step. The purified polymerase exhibits an intrinsic 3'-5' exonuclease activity and shows high activity using an oligo-primed DNA template. Neither human nor Drosophila PCNA stimulated this polymerase activity. Additional immunochemical and biochemical evidence indicates that this enzyme is distinct from DNA polymerase alpha.

Purification and partial-characterization of a protease inhibitor from Drosophila melanogaster.

A protein from Drosophila melanogaster which inhibits bovine alpha-chymotrypsin activity was purified using an extensive extraction procedure. SP-Sephadex column chromatography and affinity column chromatography. The inhibitor has an estimated molecular weight of approx. 12 000 and is extremely pH and heat stable. It did not exhibit any inhibitory activity against trypsin from numerous sources nor mosquito larval chymotrypsin but did inhibit adult mosquito chymotrypsin. Chymotrypsin-like activity has not been found in Drosophila and therefore the function of the inhibitor is unknown. Preliminary work indicates that it effectively inhibits cathepsin D activity from a nematode parasite and rabbit liver.

Studies on the mode of action of ecdysterone in adult female Aedes aegypti.

Injection of ecdysterone into non-blood fed adult female Aedes aegypti results in a marked stimulation of aromatic-L-amino-acid decarboxylase (formerly DOPA-decarboxylase) activity (Schlaeger and Fuchs, 1974a). When the hormone and alpha-amanitin are injected either simultaneously or if the toxin is administered first no inhibition of subsequent enzymatic activity is observed and in fact substantial enhancement occurs. Cordycepin injection along with ecdysterone gives results similar to alpha-amanitin. The inhibitors by themselves elicit a very small increase in DOPA decarboxylase activity compared to saline-injected controls. Conversely, actinomycin D causes severe depression of ecdysterone-mediated DOPA decarboxylase activity as dose cycloheximide and puromycin. We interpret our data to mean that the mRNA for DOPA decarboxylase is already present prior to exposure to ecdysterone. We postulate that the function of the hormone would be to modulate translation of specific pre-formed mRNA's by an unknown mechanism or to induce transcription of specific tRNAs necessary for the initation of translation of selecting existing messengers.

The ovary as a source of alpha-ecdysone in an adult mosquito.

The ovaries of the mosquito Aedes aegypti cultured in vitro secrete material that behaves like ecdysone in a radioimmunoassay. The material was identified as alpha-ecdysone by high-resolution liquid and gas-liquid chromatography. Secretion reached a maximum 16 hr after a blood meal as shown by bioassay and direct determination. Ovariectomy reduced the concentration of ecdysone in the adult after a blood meal. Qualitative analysis of whole-body extracts indicated beta-ecdysone to be the principal species present. Thus the ovaries appear to secrete a prohormone, alpha-ecdysone, which is converted to beta-ecdysone. Beta-ecdysone plays a significant role in stimulating egg development in the adult mosquito and may have reproductive roles in other insects.

Ecdysone-mediated stimulation of DOPA decarboxylase activity and its relationship to ovarian development in Aedes aegypti.

Very little dopa decarboxylase activity is detectable in adult female mosquitoes Aedes aegypti which have not been allowed to engorge blood. However, when such females are injected with the molting hormone beta-ecdysone a marked stimulation of this enzyme's activity is observable. No stimulation is observed in males similarly injected, nor in females injected with cholesterol or a juvenile hormone mimic. In addition, ecdysone injection initiates ovarian development in these anautogenous non-blood-fed mosquitoes. The extent of stimulation in both cases is dependent upon the amount of beta-ecdysone administered. These results suggested that ecdysone may play a role in ovarian development in Aedes and led us to hypothesize that a normal blood meal may trigger the synthesis, activation, or release of this hormone endogenously. Using the radioimmune assay for ecdysone developed by Borst and O'Connor (Science [Wash. D. C.] 178:4-18.), we found that the titer of an antigenic-positive material, presumably ecdysone or a closely related analogue, substantially increased 24 h after blood feeding, thereby supporting our postulation.