Microorganisms in Heat Supply Systems and Internal Corrosion of Steel Pipelines

In laboratory experiments with batch cultures of thermophilic microorganisms isolated from urban heat supply systems, the growth of sulfate-reducing, iron-oxidizing, and iron-reducing bacteria was found to accelerate the corrosion rate of the steel-3 plates used in pipelines. In the absence of bacteria and dissolved oxygen, minimal corrosion was determined. The aforementioned microorganisms, as well as sulfur-oxidizing bacteria, were found to be widespread in water and corrosion deposits in low-alloy steel pipelines (both delivery and return) of the Moscow heat networks, as well as in the corrosion deposits on the steel-3 plates in a testing unit supplied with the network water. The microorganisms were found in samples with a water pH ranging from 8.1 to 9.6 and a temperature lower than 90°C. Magnetite, lepidocrocite, goethite, and X-ray amorphous ferric oxide were the corrosion products identified on the steel-3 plates, as well as siderite, aragonite, and S⁰. The accumulation of corrosion deposits and variation in the total and local corrosion of the steel plates in a testing unit were considered in terms of the influence of microbial processes.     

Medieval example of metastatic carcinoma: a dry bone, radiological, and SEM study.

An elderly male skeleton from medieval Canterbury displayed evidence of DISH and metastatic carcinoma. The dry bone findings, SEM, and radiography suggest a primary focus in the prostate. A review of the palaeopathological literature has shown that such a finding is extremely rare in archaeological remains. This is the first reported case of prostatic carcinoma from medieval England.     

Effect of boronic acids on antifreeze proteins

The activity of antifreeze glycoprotein from the blood serum ofBoreagadus saida was strongly inhibited by ions of organic boronic acids as well as by borate. The activity of nonglycoprotein from the blood serum ofPseudopleuronectus americanus, however, was not similarly inhibited. The inhibition by borate is thus specific for molecules with the carbohydrate moiety.     

Structural,morphological, and photoluminescence properties of RE (RE = Dy3+, Eu3+, Sm3+)-doped CaAlBO4 phosphor synthesized by combustion method

The CaAlBO₄:RE (RE = Dy³⁺, Eu³⁺, Sm³⁺) phosphor were prepared via combustion synthesis and studied by X-ray diffraction (XRD), Fourier-transform infrared (FTIR) analysis, scanning electron microscopy (SEM), energy-dispersive X-ray spectroscopy (EDS), photoluminescence (PL) spectra and CIE coordinates. The phase formation of the obtained phosphor was analyzed by XRD and the result was confirmed by standard PDF Card No. 1539083. XRD data successfully indicated pure phase of CaAlBO₄ phosphor. The crystal structure of CaAlBO₄ phosphor is orthorhombic with space group Ccc2 (37). The SEM image of CaAlBO₄ phosphor reveals an agglomerated morphology and non-uniform particle size. The EDS image provides evidence of the elements present and the chemical makeup of the materials. Under the 350 nm excitation, the emission spectrum of Dy³⁺ activated CaAlBO₄ phosphor consists of two main groups of characteristic peaks located at 484 and 577 nm which are ascribed to ⁴F_9/2 → ⁶H_15/2 and ⁴F_9/2 → ⁶H_13/2 transition of Dy³⁺ respectively. The PL emission spectra of CaAlBO₄:Eu³⁺ phosphor shows characteristics bands observed around 591 and 613 nm, which corresponds to ⁵D₀ → ⁷F₁ and ⁵D₀ → ⁷F₂ transition of Eu³⁺ respectively, upon 395 nm excitation wavelength. The emission spectra of Sm³⁺ activated CaAlBO₄ phosphor shows three characteristic bands observed at 565, 601 and 648 nm which emits yellow, orange and red color. The prominent emission peak at the wavelength 601 nm, which is attributed to ⁴G_5/2 → ⁶H_7/2 transition, displays an orange emission. The CIE color coordinates of CaAlBO₄:RE (RE = Dy³⁺, Eu³⁺, Sm³⁺) phosphor are calculated to be (0.631, 0.368), (0.674, 0.325) and (0.073, 0.185). As per the obtained results, CaAlBO₄:RE (RE = Dy³⁺, Eu³⁺, Sm³⁺) phosphor may be applicable in eco-friendly lightning technology.     

Asymmetrical soft-sediment deformation structures triggered by rapid sedimentation in turbiditic deposits (Late Miocene, Guadix Basin, southern Spain)

Summary Soft-sediment deformation structures in Tortonian turbiditic deposits of the Guadix Basin (southern Spain) have been described. The most common structures are asymmetrical pillow structures and elongated sets of loadcasts. The structures are metric in scale and have been interpreted as the result of liquefaction and/or fluidization processes triggered by the rapid sedimentation of single high concentration turbidites. Final morphology of soft-sediment deformation structures is related to two main driving force systems: unstable density gradient and lateral shear stress. The latter is probably induced by the downslope component of the sediment weight. The asymmetry of deformational structures (in horizontal and vertical cross-section) allows a clarification of the relationship between morphology of deformation and direction of lateral shear stress: this relationship seems ambiguous and confused in the literature. The interpretations both of deformation mechanism and trigger agent have been supported with:-field analyses;-calculations on the liquefaction processes induced by rapid sedimentation;-qualitative models in laboratory.     

Neuronal loss and microgliosis are restricted to the core of Aβ deposits in mouse models of Alzheimer's disease

Amyloid‐β (Aβ) deposits, pathologic tau, and neurodegeneration are major pathological hallmarks of Alzheimer''s disease (AD). The relationship between neuronal loss and Aβ deposits is one of the fundamental questions in the pathogenesis of AD. However, this relationship is controversial. One main reason for the conflicting results may be the confounding effects of pathologic tau, which often coexists with Aβ deposits in the brains of AD patients. To clarify the relationship between neuronal loss and Aβ deposits, mouse models of AD, which develop abundant Aβ deposits in the aged brain without pathologic tau, were used to examine the co‐localization of NeuN‐positive neurons, NF‐H‐positive axons, MBP‐positive myelin sheaths, and Aβ deposits. Neuronal loss, as measured by decreased staining of the neuronal cell body, axon, and myelin sheath, as well as the IBA‐1‐positive microglia, was significantly increased in the core area of cerebral Aβ deposits, but not in adjacent areas. Furthermore, neuronal loss in the core area of cerebral Aβ deposits was correlated with Aβ deposit size. These results clearly indicate that neuronal loss is restricted to the core of Aβ deposits, and this restricted loss probably occurs because the Aβ deposit attracts microglia, which cluster in the core area where Aβ toxicity and neuroinflammation toxicity are restrained. These findings may contribute to our understanding of the relationship between neuronal loss and Aβ deposits in the absence of pathologic tau.     

A Monoclonal Antibody That Reacts Immunohistochemically with Amyloid Deposits in the Brain Tissue of Alzheimer Patients Binds to an Epitope Present on Complement Factor 4

The mouse monoclonal antibody SMP has previously been demonstrated to react immunohistochemically with neurofibrillary tangles, argyrophilic plaques, and leptomeningeal vascular amyloid deposits in the brain tissue of individuals dying from pathologically diagnosed Alzheimer's disease. In preliminary studies the antibody was shown, by size exclusion chromatography, to bind to a protein with an apparent molecular mass of 260 kDa present in the CSF and serum of demented individuals. Chromatographic separation of a 40% ammonium sulphate precipitate of CSF and serum yielded immunoreactive fractions that were subjected to 9% sodium dodecyl sulphate-polyacrylamide gel electrophoresis followed by western blotting. Probing the nitrocellulose blot with the antibody revealed that the antibody selectively binds to a protein chain with an apparent molecular mass of 100 kDa. By using a combination of affinity chromatography and sodium dodecyl sulphate-polyacrylamide gel electrophoresis, coupled with western blotting, the serum component with which the antibody reacts has been identified as complement factor 4. In addition, the antibody has been shown to react specifically with an epitope on the alpha-chain of this protein.