Dehydrogenase Enzymes Associated to Glycolysis in Beef Carcasses Stored at 0 °C

After the death of an animal, cell metabolism is controlled locally. The post-mortem oxygen depletion increases the glycolytic activity and lactate production. However, many mechanisms of post-mortem metabolic regulation have not been fully investigated in beef carcasses. In this work, we studied the post-mortem glycolytic behavior (including lactate dehydrogenase) and three dehydrogenase associated to glycolysis (glycerophosphate dehydrogenase, glucose 6-phosphate dehydrogenase, and glycerol dehydrogenase) by using cytochemistry techniques in three fast-twitch muscles (M. longissimus dorsi, M. semimembranosus, and M. cutaneus trunci) of carcasses stored at 0 °C. Our results indicate that glycolysis depends on the type of muscle. The post-mortem glycolytic flux and lactate dehydrogenase activity of M. cutaneus trunci was the lowest of the three muscles studied. Of the other dehydrogenases analyzed, only glycerophosphate and glycerol dehydrogenase showed clear cytochemical reaction. Glucose 6-phosphate dehydrogenase was not used by muscles very much. The glycerophosphate dehydrogenase was the strongest enzymatic activity correlated to the post-mortem glycolytic flux. In addition, a relationship between glycerophosphate dehydrogenase and glycerol dehydrogenase was detected by using a multiple regression model. This phenomenon was studied by using bioinformatics tools, suggesting that glycerophosphate dehydrogenase could oxidize the glycerol in bovine fast-twitch muscles.     

Site‐Selectively Coated,Densely‐Packed Microprojection Array Patches for Targeted Delivery of Vaccines to Skin

Densely packed dry‐coated microprojections are shown to deliver vaccines to targeted locations within the skin that are rich in immune cells, thus inducing protective immune responses against a lethal virus challenge. Selectively limiting the antigen coating to the tips of the projections, which penetrate the skin, would significantly reduce the amount of vaccine required in immunization. In this paper a simple technique, dip‐coating the microprojections, is introduced to meet this goal. By increasing the coating solution viscosity, an otherwise strong capillary action is mitigated and the desired controlled coating length on projections is achieved. Following application to the skin, most of the coated vaccine material is rapidly released from the projections (82.6% in mass within 2 min) to the target locations within the skin strata and a potent immune response is induced when a conventional influenza vaccine (Fluvax) is tested in a mouse model. The utility of this coating approach to a variety of molecules representative of vaccines (e.g., chicken egg ovalbumin (OVA) protein, DNA, and fluorescent dyes) is demonstrated. These collective attributes, together with the simplicity of the approach, position the dip‐coating method for practical utility in large vaccination campaigns.     

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation,Radical Production and Reduces Aβ Toxicity

Amyloid‐β peptides (Aβ) and the protein human serum albumin (HSA) interact in vivo. They are both localised in the blood plasma and in the cerebrospinal fluid. Among other functions, HSA is involved in the transport of the essential metal copper. Complexes between Aβ and copper ions have been proposed to be an aberrant interaction implicated in the development of Alzheimer's disease, where Cu is involved in Aβ aggregation and production of reactive oxygen species (ROS). In the present work, we studied copper‐exchange reaction between Aβ and HSA or the tetrapeptide DAHK (N‐terminal Cu‐binding domain of HSA) and the consequence of this exchange on Aβ‐induced ROS production and cell toxicity. The following results were obtained: 1) HSA and DAHK removed Cu^II from Aβ rapidly and stoichiometrically, 2) HSA and DAHK were able to decrease Cu‐induced aggregation of Aβ, 3) HSA and DAHK suppressed the catalytic HO^. production in vitro and ROS production in neuroblastoma cells generated by Cu–Aβ and ascorbate, 4) HSA and DAHK were able to rescue these cells from the toxicity of Cu–Aβ with ascorbate, 5) DAHK was more potent in ROS suppression and restoration of neuroblastoma cell viability than HSA, in correlation with an easier reduction of Cu^II–HSA than Cu–DAHK by ascorbate, in vitro. Our data suggest that HSA is able to decrease aberrant Cu^II–Aβ interaction. The repercussion of the competition between HSA and Aβ to bind Cu in the blood and brain and its relation to Alzheimer's disease are discussed.     

Influence of current density on crystalline structure and magnetic properties of electrodeposited Co-rich CoNiW alloys

The influence of current density, at the interval 5–100 mA cm⁻², on the structural and magnetic properties of electrodeposited (Co_100−xNi_x)_100−yW_y alloys (x = 23–33.5 at. % Ni, y = 1.7–7.3 at. % W) was studied from a glycine-containing bath. W-content decreases with the increase of the current density magnitude. X-ray data have shown stabilization of hexagonal close packed, face centered cubic or a mixture of these structures by modulating the applied cathodic current density, for values lower than 50 mA cm⁻². Two structural phase transitions were observed: one from hexagonal close packed to face centered cubic structural transition occurring for a current density of 20 mA cm⁻², and another one, from cubic crystalline phase to amorphous state, which happens for values higher than 50 mA cm⁻². These structural phase transitions seem to be associated with the W-content as well as average crystalline grain sizes that reduce with increasing the current density value. The grain size effect may explain the face centered cubic stabilization in Co-rich CoNiW alloys, which was initially assumed to be basically due to H-adsorption/incorporation. Magnetic properties of Co-rich CoNiW alloys are strongly modified by the current density value; as a result of the changes on the W-content and their structural properties.     

Proton binding onto soil by nonelectrostatic models: isolation and identification of mineral contributions

In this paper a methodological approach is proposed to validate mechanistic modeling for proton binding onto active sites of mineral and soil samples by reducing the uncertainty and arbitrariness of model schematization. This approach is based on the quantitative formulation (X-ray calibration method) of a simulating mineral mixture (SMM) accounting for the main mineral phases in the soil (quartz, goethite, hematite, muscovite, clinochlore). Mineral and organic contributions were separated by comparing titration curves of river sediment and SMM. Specific mineral contributions to the acid properties of SMM were separated by comparing titration models of SMM and single minerals. Different nonelectrostatic models were used for titrations of SMM and single minerals: two-site/three-KH models (one amphoteric plus one monoprotic site) for clay minerals and SMM; one-site/two-KH models (one amphoteric site) for goethite and hematite; and a one-site/one-KH model (one monoprotic site) for quartz. Crossed-comparisons of titration models allow for identifying and quantifying the specific contributions of the distinct edge hydroxyl groups of iron oxides, clay minerals, and quartz in the different pH ranges. In particularthe amphoteric sites of aluminosilicates mainly contribute in the acid-neutral pH range, the amphoteric sites of iron oxides take part in the neutral-basic range, and finally the monoprotic edge hydroxyl groups of quartz react in the upper basic region of pH. The good simulation of the acid-base properties of SMM (according to single mineral titration models and quantitative composition by X-ray) confirms both model schematization and SMM formulation. Speciation diagrams of the active sites of the different mineral components (aluminosilicates, iron oxides, and quartz) were obtained by implementing the database of a dedicated software with the apparent equilibrium constants regressed by titration modeling of single minerals.     

Storage stability of liver oil from two ray (Rhinoptera bonasus and Aetobatus narinari) species from the Gulf of Mexico

The effect of storage time on the quality of liver oil from two commercial rajiform species (Rhinoptera bonasus and Aetobatus narinari) captured in the Gulf of Mexico (State of Campeche coast line) was evaluated. Oil characterisation was conducted by physical (specific gravity, saponification index and water content) and chemical analyses (fatty acid content, carotenes and tocopherols) whilst storage stability (peroxide value, free fatty acids, conjugated dienes, anisidine value and changes in docosahexaenoic acid, DHA and content) was studied for 87 days at 25 °C. Increases (p < 0.05) in free fatty acids, conjugated dienes, peroxide value and anisidine value, and a decrease (p < 0.05) in DHA were observed during the storage time for both oil species as oxidation proceeded. It was concluded that R. bonasus and A. narinari oils lasted for 52 and 66 days under these storage conditions, respectively.     

Hydrotalcite-like compounds obtained by anion exchange reactions

The synthesis of nickel aluminium hydroxypicrate, [Ni₃Al(OH)₈] (C₆O₇N₃H₂)·nH ₂O, and lithium aluminium hydroxypicrate, [Al₂Li(OH)₆] (C₆O₇N₃H₂)·nH ₂O by anion exchange is described. Picric acid and the corresponding hydroxycarbonates were used as starting materials. The new compounds were characterized by chemical analyses, electron microscopy, infrared spectroscopy and X-ray diffraction. The results obtained indicate that both are hydrotalcite-like compounds where the picrate anion lies between the basic layers. The thermal decomposition of the compounds was studied by differential thermal and thermogravimetric analysis.     

Surface hydrophobicity and functional properties of myofibrillar proteins of mantle from frozen-stored squid (Illex argentinus) caught either jigging machine or trawling

The surface hydrophobicity and functional properties of actomyosin from the mantle of frozen squid caught either by jigging machines (AME1) or by trawl (AME2) were investigated. Two components of 155 and 55 kDa were present in the gels at zero time of storage. Degradation of the myosin heavy chain and increase in the 155 kDa component occur earlier in AME2. Irrespective of the catch method used, no significant (P>0.05) changes in protein solubility were observed. The reduced viscosity of both AME1 and AME2 decreased up to months 3 and 5 of frozen storage, respectively. At the beginning of storage, the superficial hydrophobicity of AME2 was 30% higher than that of AME1. So 1-anilino-8-naphthalene sulfonic acid of AME2 significantly increased during 3-5 months of storage period and that of AME1 at the end of storage. The emulsion activity index (EAI) of AME2 significantly (P<0.05) increased during the first month and decreased after 3 months of storage. EAI of AME1 decreased at month 3 and remained unchanged thereafter. Emulsion stability (ES) of AME2 showed a behavior that was similar to its IAE and that of AME1 remained unchanged.