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Hen Egg White Lysozyme (hen + egg_white_lysozyme)
Selected AbstractsGrowth of large protein crystals by a large-scale hanging-drop methodJOURNAL OF APPLIED CRYSTALLOGRAPHY, Issue 4 2010Keisuke Kakinouchi A method for growing large protein crystals is described. In this method, a cut pipette tip is used to hang large-scale droplets (maximum volume 200,µl) consisting of protein and precipitating agents. A crystal grows at the vapor,liquid interface; thereafter the grown crystal can be retrieved by droplet,droplet contact both for repeated macroseeding and for mounting crystals in a capillary. Crystallization experiments with peroxiredoxin of Aeropyrum pernix K1 (thioredoxin peroxidase, ApTPx) and hen egg white lysozyme demonstrated that this large-scale hanging-drop method could produce a large-volume crystal very effectively. A neutron diffraction experiment confirmed that an ApTPx crystal (6.2,mm3) obtained by this method diffracted to beyond 3.5,Å resolution. [source] A simple technique to convert sitting-drop vapor diffusion into hanging-drop vapor diffusion by solidifying the reservoir solution with agaroseJOURNAL OF APPLIED CRYSTALLOGRAPHY, Issue 5 2009Tae Woong Whon A simple protocol to convert sitting-drop vapor-diffusion plating into a hanging-drop vapor-diffusion experiment in protein crystallization is reported. After making a sitting-drop plate, agarose solution was added to solidify the reservoir solution, and the plates were incubated upside down. Crystallization experiments with hen egg white lysozyme, thaumatin and glucose isomerase showed that the `upside-down sitting-drop' method could produce single crystals with all the benefits of the hanging-drop crystallization method. [source] Soluble oligomers from a non-disease related protein mimic A,-induced tau hyperphosphorylation and neurodegenerationJOURNAL OF NEUROCHEMISTRY, Issue 2 2007Marcelo N. N. Vieira Abstract Protein aggregation and amyloid accumulation in different tissues are associated with cellular dysfunction and toxicity in important human pathologies, including Alzheimer's disease and various forms of systemic amyloidosis. Soluble oligomers formed at the early stages of protein aggregation have been increasingly recognized as the main toxic species in amyloid diseases. To gain insight into the mechanisms of toxicity instigated by soluble protein oligomers, we have investigated the aggregation of hen egg white lysozyme (HEWL), a normally harmless protein. HEWL initially aggregates into ,-sheet rich, roughly spherical oligomers which appear to convert with time into protofibrils and mature amyloid fibrils. HEWL oligomers are potently neurotoxic to rat cortical neurons in culture, while mature amyloid fibrils are little or non-toxic. Interestingly, when added to cortical neuronal cultures HEWL oligomers induce tau hyperphosphorylation at epitopes that are characteristically phosphorylated in neurons exposed to soluble oligomers of the amyloid-, peptide. Furthermore, injection of HEWL oligomers in the cerebral cortices of adult rats induces extensive neurodegeneration in different brain areas. These results show that soluble oligomers from a non-disease related protein can mimic specific neuronal pathologies thought to be induced by soluble amyloid-, peptide oligomers in Alzheimer's disease and support the notion that amyloid oligomers from different proteins may share common structural determinants that would explain their generic cytotoxicities. [source] Novel Isoelectric Precipitation of Proteins in a Pressurized Carbon Dioxide-Water-Ethanol SystemBIOTECHNOLOGY PROGRESS, Issue 4 2004Xiang-Ming Qi A novel isoelectric precipitation of proteins in a pressurized carbon dioxide,water,ethanol system was developed where carbon dioxide was used as a volatile acid. The pH,pressure curves of the system with the absence and presence of proteins were investigated. By introducing the pressurized carbon dioxide to a solution containing protein, the pH value in the solution was decreased to the isoelectric region of the model protein BSA. Addition of ethanol could lower the buffer capacity of the protein, which made the precipitation concentration of protein go beyond the limits in a system without ethanol and well exploited the application field of the technique. In addition, ethanol in solution played the role of aiding precipitation in the process. Another model protein, hen egg white lysozyme, was also studied but could not be precipitated in the above system. All of these phenomena prove that isoelectric precipitation is the key point in the pressurized carbon dioxide,water,ethanol system. [source] | ||||||||||