787 resultados para Logistics organizational stages


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In this study ,the effects of Pseudomonas fluorescence obtained from generator pond water of Kolahi as supplementary and four algae consisting of : Chaetoceros sp, Chlorella and Skeletonema sp and Tetraselmis sp, three types of artemia as live food larval states from zoa to postlarvae (PL4 ) Penaeus indicus were investigated. The results indicate that Pseudomonas fluorescence has positive effect on Penaeus indicits larvae growth and their living food. Effective ranges at minimum and maximum were estimated. In most cases optimum dosage was approximately determined. Optimum dosage is between 50 -150 milligrams per liter for living food and Penaeus larval More than 200 milligram per liter resulted in a negative effect on the growth and survival. Also the results indicate Uromiana artemia. Requires a higher concentration of the bacteria the imported artemia. As a conclusion it is recommended to introduce Pseudonionas fluorescence as a new medium for the growth of some mentioned algae .

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To investigation of the toxic effects of atrazine on newly hatched larvae and releasing age fry of the Caspian Kutum, Rutilus frisii kutum, the 96h LC50 was determined as 18.53 ppm and 24.95 ppm, respectively. Newly hatched larvae were exposed to three sublethal concentrations of atrazine (1/2LC50, 1/4LC50 and 1/8LC50) for 7 days. Different histopathological alterations were observed in fins and integument, gills, Kidney, digestive system, liver and the brain of the exposed larvae. Fry’s were exposed to one sublethal concentration of atrazine (1/2LC50) for four days, and like the larvae’s, many histopathological alterations were observed in fins and integument, gills, Kidney, digestive system, liver and the brain of the exposed fry’s, too. Also, measurements of the body ions: Na+, K+, Ca2+, Mg2+ and Cl- in atrazine exposed larvae and fry’s compare to control groups showed that atrazine is changed the body ions composition. No significant differences were found in length growth rate, weight growth rate and the condition factor of the atrazine exposed larvae and fry. Immunohistochemical localization of the Na+, K+-ATPase in integumentary and gill ionocytes, showed no differences in dispersion pattern of the ionocytes in atrazine exposed larvae and fry, compare to control group. Measuring the dimensions of the ionocytes and counting the ionocytes showed that atrazine is affecting on ionocytes by mild increasing in size and mild decreasing in number. Ultrastructural studies, using SEM and TEM, showed that atrazine have significant effects on cellular and subcellular properties. It caused necrosis in surface of the pavement cells in branchial epithelium, necrosis in endoplasmic reticulum of the ionocytes and changed the shape of the mitochondria in these cells. Results showed that sublethal concentrations of atrazine were very toxic to larvae and fry of the Rutilus frisii kutum, and at these levels can made some serious histopathological alterations in their tissues. Related to the severe histopathological alterations in osmoregulatory organs, like gill, kidney and digestive system, and the alterations in the body ion composition, it could be concluded that atrazine could interfere with the osmoregulation process of the Rutilus frisii kutum at the early stages of the life history.

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Scalable growth is essential for graphene-based applications. Recent development has enabled the achievement of the scalability by use of chemical vapor deposition (CVD) at 1000°C with copper as a catalyst and methane as a precursor gas. Here we report our observation of early stage of graphene growth based on an ethylene-based CVD method, capable of reducing the growth temperature to 770°C for monolayer graphene growth on copper. We track the early stages of slow growth under low ethylene flow rate and observe the graphene domain evolution by varying the temperature and growth time. Temperature-dependence of graphene domain density gives an apparent activation energy of 1.0 eV for nucleation.

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Nanobodies are single-domain fragments of camelid antibodies that are emerging as versatile tools in biotechnology. We describe here the interactions of a specific nanobody, NbSyn87, with the monomeric and fibrillar forms of α-synuclein (αSyn), a 140-residue protein whose aggregation is associated with Parkinson's disease. We have characterized these interactions using a range of biophysical techniques, including nuclear magnetic resonance and circular dichroism spectroscopy, isothermal titration calorimetry and quartz crystal microbalance measurements. In addition, we have compared the results with those that we have reported previously for a different nanobody, NbSyn2, also raised against monomeric αSyn. This comparison indicates that NbSyn87 and NbSyn2 bind with nanomolar affinity to distinctive epitopes within the C-terminal domain of soluble αSyn, comprising approximately amino acids 118-131 and 137-140, respectively. The calorimetric and quartz crystal microbalance data indicate that the epitopes of both nanobodies are still accessible when αSyn converts into its fibrillar structure. The apparent affinities and other thermodynamic parameters defining the binding between the nanobody and the fibrils, however, vary significantly with the length of time that the process of fibril formation has been allowed to progress and with the conditions under which formation occurs, indicating that the environment of the C-terminal domain of αSyn changes as fibril assembly takes place. These results demonstrate that nanobodies are able to target forms of potentially pathogenic aggregates that differ from each other in relatively minor details of their structure, such as those associated with fibril maturation.

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This paper proposes a method for analysing the operational complexity in supply chains by using an entropic measure based on information theory. The proposed approach estimates the operational complexity at each stage of the supply chain and analyses the changes between stages. In this paper a stage is identified by the exchange of data and/or material. Through analysis the method identifies the stages where the operational complexity is both generated and propagated (exported, imported, generated or absorbed). Central to the method is the identification of a reference point within the supply chain. This is where the operational complexity is at a local minimum along the data transfer stages. Such a point can be thought of as a 'sink' for turbulence generated in the supply chain. Where it exists, it has the merit of stabilising the supply chain by attenuating uncertainty. However, the location of the reference point is also a matter of choice. If the preferred location is other than the current one, this is a trigger for management action. The analysis can help decide appropriate remedial action. More generally, the approach can assist logistics management by highlighting problem areas. An industrial application is presented to demonstrate the applicability of the method. © 2013 Operational Research Society Ltd. All rights reserved.

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Nanobodies are single-domain fragments of camelid antibodies that are emerging as versatile tools in biotechnology. We describe here the interactions of a specific nanobody, NbSyn87, with the monomeric and fibrillar forms of α-synuclein (αSyn), a 140-residue protein whose aggregation is associated with Parkinson's disease. We have characterized these interactions using a range of biophysical techniques, including nuclear magnetic resonance and circular dichroism spectroscopy, isothermal titration calorimetry and quartz crystal microbalance measurements. In addition, we have compared the results with those that we have reported previously for a different nanobody, NbSyn2, also raised against monomeric αSyn. This comparison indicates that NbSyn87 and NbSyn2 bind with nanomolar affinity to distinctive epitopes within the C-terminal domain of soluble αSyn, comprising approximately amino acids 118-131 and 137-140, respectively. The calorimetric and quartz crystal microbalance data indicate that the epitopes of both nanobodies are still accessible when αSyn converts into its fibrillar structure. The apparent affinities and other thermodynamic parameters defining the binding between the nanobody and the fibrils, however, vary significantly with the length of time that the process of fibril formation has been allowed to progress and with the conditions under which formation occurs, indicating that the environment of the C-terminal domain of αSyn changes as fibril assembly takes place. These results demonstrate that nanobodies are able to target forms of potentially pathogenic aggregates that differ from each other in relatively minor details of their structure, such as those associated with fibril maturation. © 2013 Elsevier Ltd.