Academic literature on the topic 'Equine Lysozyme (EL)'

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Journal articles on the topic "Equine Lysozyme (EL)"

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Morozova, Ludmilla, Petra Haezebrouck, and Frans Van Cauwelaert. "Stability of equine lysozyme." Biophysical Chemistry 41, no. 2 (1991): 185–91. http://dx.doi.org/10.1016/0301-4622(91)80018-m.

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Nitta, Katsutoshi, Hideaki Tsuge, Shintaro Sugai, and Keiichi Shimazaki. "The calcium-binding property of equine lysozyme." FEBS Letters 223, no. 2 (1987): 405–8. http://dx.doi.org/10.1016/0014-5793(87)80328-9.

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Haezebrouck, P., and H. Van Dael. "The folding-unfolding transition of equine lysozyme." Journal of Molecular Structure 294 (March 1993): 143–45. http://dx.doi.org/10.1016/0022-2860(93)80335-s.

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PRIYADARSHINI, SUBHADRA, and VINOD K. KANSAL. "Purification, characterization, antibacterial activity and N-terminal sequencing of buffalo-milk lysozyme." Journal of Dairy Research 69, no. 3 (2002): 419–31. http://dx.doi.org/10.1017/s002202990200554x.

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Lysozyme from buffalo milk was purified to homogeneity and its N-terminal amino acid sequence, biochemical properties and antibacterial spectrum were determined. The purification procedure, comprising ion-exchange chromatography using CM-cellulose and size-exclusion chromatography using Sephadex G-50, conferred 8622-fold purification and 39·3% recovery of lysozyme. The purified enzyme migrated as a single band on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and native PAGE. Immunological purity of lysozyme preparation was confirmed by immuno-electrophoresis. Molecular
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Nakao, Masaharu, Munehito Arai, Takumi Koshiba, Katsutoshi Nitta, and Kunihiro Kuwajima. "Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy." Spectroscopy 17, no. 2-3 (2003): 183–93. http://dx.doi.org/10.1155/2003/184135.

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We have studied the guanidine hydrochloride‒induced equilibrium unfolding and the kinetics of refolding of canine milk lysozyme by circular dichroism and fluorescence spectroscopy. The thermodynamic analysis of the equilibrium unfolding measured by circular dichroism and fluorescence has shown that unfolding is represented by a three‒state mechanism and that the intermediate state of canine milk lysozyme is remarkably more stable than the intermediates observed in other lysozyme and α-lactalbumin. In the kinetic refolding of this protein, there are at least two kinetic intermediates; a burst=p
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Griko, Yuri V., Ernesto Freire, George Privalov, Herman Van Dael, and Peter L. Privalov. "The Unfolding Thermodynamics of c-Type Lysozymes: A Calorimetric Study of the Heat Denaturation of Equine Lysozyme." Journal of Molecular Biology 252, no. 4 (1995): 447–59. http://dx.doi.org/10.1006/jmbi.1995.0510.

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Casaite, V., S. Bruzyte, V. Bukauskas, A. Setkus, L. A. Morozova-Roche, and R. Meskys. "Expression and purification of active recombinant equine lysozyme in Escherichia coli." Protein Engineering Design and Selection 22, no. 11 (2009): 649–54. http://dx.doi.org/10.1093/protein/gzp048.

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Haezebrouck, Petra, Wim Noppe, Herman Van Dael та Ignace Hanssens. "Hydrophobic interaction of lysozyme and α-lactalbumin from equine milk whey". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1122, № 3 (1992): 305–10. http://dx.doi.org/10.1016/0167-4838(92)90409-7.

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Masty, J., and R. P. Stradley. "Paneth cell degranulation and lysozyme secretion during acute equine alimentary laminitis." Histochemistry 95, no. 5 (1991): 529–33. http://dx.doi.org/10.1007/bf00315751.

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Morozova-Roche, Ludmilla A., Jonathan A. Jones, Wim Noppe, and Christopher M. Dobson. "Independent Nucleation and Heterogeneous Assembly of Structure During Folding of Equine Lysozyme." Journal of Molecular Biology 289, no. 4 (1999): 1055–73. http://dx.doi.org/10.1006/jmbi.1999.2741.

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Dissertations / Theses on the topic "Equine Lysozyme (EL)"

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Wilhelm, Kristina Rebecca. "Protein complexes assembly, structure and function /." Umeå : Umeå university, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-29792.

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Book chapters on the topic "Equine Lysozyme (EL)"

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Vukojević, Vladana, Alexei Klechikov, and Ludmilla A. Morozova-Roche. "ELOA – Equine Lysozyme Complexes with Oleic Acid." In Bio-nanoimaging. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-394431-3.00040-7.

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Reports on the topic "Equine Lysozyme (EL)"

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Noga, Edward J., Ramy R. Avtalion, and Michael Levy. Comparison of the Immune Response of Striped Bass and Hybrid Bass. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568749.bard.

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We developed methods for examining the pathophysical response of striped bass and hybrid bass to various forms of stress. This involved development of techniques for the measurement of lysozyme, mitogen blastogenesis, mixed lymphocyte reaction, and oxidative burst, which are important general indicators of systemic immune function. We also examined local immune defenses (epithelial integrity), as well as homeostatic indicators in blood, including osmotic balance and glucose. Acute stress resulted in significant perturbations in a number of parameters, including glucose, electrolytes, osmolarit
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