The geochemistry of pore water in the till underlying the infiltr

The geochemistry of pore water in the till underlying the infiltration pond was determined prior to filling with process-affected

water (2008) and two years after the infiltration pond was filled with PA waters (2010). Pore water was analyzed for metals, cations, anions, and isotopes (H-2 and O-18). The distribution of conservative tracers (O-18 and chloride) indicated migration of the PA waters to approximately 0.9 m, but the migrations of major ions and metals were significantly delayed relative to this depth. Uptake of Na and Mo and release of Ca, Mg, Mn, Ba, and Sr suggest that adsorption and ion exchange reactions are the foremost attenuation processes controlling p38 protein kinase inorganic solutes EGFR inhibitor transport. (C) 2013 Elsevier B.V. All rights reserved.”
“A novel method, based on acoustic emission (AE) techniques, for detecting agglomeration in fluidized beds is presented. Particle size characteristics are determined based on the principle that AE signals

with different frequency band energies are emitted when particles of different sizes impact an internal wall. By applying chaotic analysis to the AE signals, the malfunction coefficients are well defined. Agglomeration in the fluidized bed can then be detected by the sudden variation of malfunction coefficients. AE signals were investigated in a laboratory scale heated fluidized bed and an industrial polyethylene fluidized bed. Experimental data showed that the malfunction coefficients increased

with the growth of agglomeration. The results indicated that agglomeration in fluidized beds can be predicted and diagnosed effectively and precisely using AE techniques based on chaotic analysis.”
“Tissue inhibitor of metalloproteinases-1 (TIMP-1) is an endogenous inhibitor of matrix metalloproteinases (MMPs) with reported tumor promoting, as well as inhibitory, effects. These paradoxical properties are presumably mediated by different biological functions, MMP-dependent as well as -independent, and probably related to TIMP-1 levels of protein expression, ON-01910 in vitro post-translational modifications, and cellular localization. TIMP-1 is an N-glycosylated protein that folds into two functional domains, a C- and an N-terminal domain, with six disulfide bonds. Furthermore, TIMP-1 is processed in the N-terminal sequence. These three biochemical properties make TIMP-1 difficult to produce in conventional bacterial, insect, or yeast expression systems. We describe here a HEK293 cell-based strategy for production and purification of secreted and N-glycosylated recombinant his(6)-tagged human TIMP-1 (his(6)-rTIMP-1), which resulted in large amounts of highly purified and bioactive protein. Matrix-assisted laser desorption ionization mass spectrometry confirmed the N- and C-termini of his(6)-rTIMP-1, and N-glycosylation profiling showed a match to the N-glycosylation of human plasma TIMP-1.

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