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

Author: Grafiati

Published: 7 June 2025

Last updated: 2 August 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Tsuge, Hideaki, Hideo Ago, Masana Noma, Katsutoshi Nitta, Shintaro Sugai, and Masashi Miyano. "Crystallographic Studies of a Calcium Binding Lysozyme from Equine Milk at 2.5 ÅResolution." Journal of Biochemistry 111, no. 2 (1992): 141–43. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a123727.

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12

Van Dael, Herman, Petra Haezebrouck, Ludmilla Morozova, Christopher Arico-Muendel, and Christopher M. Dobson. "Partially folded states of equine lysozyme. Structural characterization and significance for protein folding." Biochemistry 32, no. 44 (1993): 11886–94. http://dx.doi.org/10.1021/bi00095a018.

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13

Tsuge, Hideaki, Koushi Koseki, Masashi Miyano, et al. "A structural study of calcium-binding equine lysozyme by two-dimensional 1H-NMR." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1078, no. 1 (1991): 77–84. http://dx.doi.org/10.1016/0167-4838(91)90095-h.

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14

Morozova-Roche, Ludmilla A. "Equine lysozyme: The molecular basis of folding, self-assembly and innate amyloid toxicity." FEBS Letters 581, no. 14 (2007): 2587–92. http://dx.doi.org/10.1016/j.febslet.2007.05.023.

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15

Morozova-Roche, Ludmilla A., Christopher C. Arico-Muendel, Donald T. Haynie, Viktor I. Emelyanenko, Herman Van Dael, and Christopher M. Dobson. "Structural characterisation and comparison of the native and A-states of equine lysozyme." Journal of Molecular Biology 268, no. 5 (1997): 903–21. http://dx.doi.org/10.1006/jmbi.1997.0996.

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16

Blanch, Ewan W., Ludmilla A. Morozova-Roche, Lutz Hecht, Wim Noppe та Laurence D. Barron. "Raman optical activity characterization of native and molten globule states of equine lysozyme: Comparison with hen lysozyme and bovine α-lactalbumin". Biopolymers 57, № 4 (2000): 235–48. http://dx.doi.org/10.1002/1097-0282(2000)57:4<235::aid-bip5>3.0.co;2-h.

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17

Noppe, W., I. Hanssens, and M. De Cuyper. "Simple two-step procedure for the preparation of highly active pure equine milk lysozyme." Journal of Chromatography A 719, no. 2 (1996): 327–31. http://dx.doi.org/10.1016/0021-9673(95)00677-x.

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18

Clementi, Emily A., Kristina R. Wilhelm, Jürgen Schleucher, Ludmilla A. Morozova-Roche, and Anders P. Hakansson. "A Complex of Equine Lysozyme and Oleic Acid with Bactericidal Activity against Streptococcus pneumoniae." PLoS ONE 8, no. 11 (2013): e80649. http://dx.doi.org/10.1371/journal.pone.0080649.

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19

Mizuguchi, Mineyuki, Munehito Arai, Yue Ke, Katsutoshi Nitta, and Kunihiro Kuwajima. "Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy." Journal of Molecular Biology 283, no. 1 (1998): 265–77. http://dx.doi.org/10.1006/jmbi.1998.2100.

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20

Wilhelm, Kristina, Adas Darinskas, Wim Noppe, et al. "Protein oligomerization induced by oleic acid at the solid-liquid interface - equine lysozyme cytotoxic complexes." FEBS Journal 276, no. 15 (2009): 3975–89. http://dx.doi.org/10.1111/j.1742-4658.2009.07107.x.

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21

Yasui, Tadashi, Kousuke Fukui, Takayuki Nara, Isao Habata, Wilfried Meyer та Azuma Tsukise. "Immunocytochemical localization of lysozyme and β-defensin in the apocrine glands of the equine scrotum". Archives of Dermatological Research 299, № 8 (2007): 393–97. http://dx.doi.org/10.1007/s00403-007-0766-5.

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22

Desmet, Johan, Herman Van Dael, Frans Van Cauwelaert, Katsutoshi Nitta та Shintaro Sugai. "Comparison of the binding of Ca2+ and Mn2+ to bovine α-lactalbumin and equine lysozyme". Journal of Inorganic Biochemistry 37, № 3 (1989): 185–91. http://dx.doi.org/10.1016/0162-0134(89)80041-8.

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23

Pellegrini, A., S. Waiblinger, and R. von Fellenberg. "Purification of equine neutrophil lysozyme and its antibacterial activity against Gram-positive and Gram-negative bacteria." Veterinary Research Communications 15, no. 6 (1991): 427–35. http://dx.doi.org/10.1007/bf00346538.

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24

Vukojević, Vladana, Alice M. Bowen, Kristina Wilhelm, et al. "Lipoprotein Complex of Equine Lysozyme with Oleic Acid (ELOA) Interactions with the Plasma Membrane of Live Cells." Langmuir 26, no. 18 (2010): 14782–87. http://dx.doi.org/10.1021/la1026416.

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25

Cieslak, Jakub, Lukasz Wodas, Alicja Borowska, et al. "Variability of lysozyme and lactoferrin bioactive protein concentrations in equine milk in relation toLYZandLTFgene polymorphisms and expression." Journal of the Science of Food and Agriculture 97, no. 7 (2016): 2174–81. http://dx.doi.org/10.1002/jsfa.8026.

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26

Permyakov, Sergei E., Tatyana I. Khokhlova, Aliya A. Nazipova, Andrey P. Zhadan, Ludmila A. Morozova-Roche, and Eugene A. Permyakov. "Calcium-binding and temperature induced transitions in equine lysozyme: New insights from the pCa-temperature “phase diagrams”." Proteins: Structure, Function, and Bioinformatics 65, no. 4 (2006): 984–98. http://dx.doi.org/10.1002/prot.21159.

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27

Spencer, Andrew, Ludmilla A. Morozov-Roche, Wim Noppe, et al. "Expression, Purification, and Characterization of the Recombinant Calcium-Binding Equine Lysozyme Secreted by the Filamentous FungusAspergillus niger:Comparisons with the Production of Hen and Human Lysozymes." Protein Expression and Purification 16, no. 1 (1999): 171–80. http://dx.doi.org/10.1006/prep.1999.1036.

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28

Mizuguchi, Mineyuki, Masayuki Nara, Yue Ke, Keiichi Kawano, Toshifumi Hiraoki, and Katsutoshi Nitta. "Fourier-Transform Infrared Spectroscopic Studies on the Coordination of the Side-Chain COO- Groups to Ca2+ in Equine Lysozyme." European Journal of Biochemistry 250, no. 1 (1997): 72–76. http://dx.doi.org/10.1111/j.1432-1033.1997.00072.x.

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29

Mizuguchi, Mineyuki, Kazuo Masaki та Katsutoshi Nitta. "The molten globule state of a chimera of human α-lactalbumin and equine lysozyme 1 1Edited by P. E. Wright". Journal of Molecular Biology 292, № 5 (1999): 1137–48. http://dx.doi.org/10.1006/jmbi.1999.3132.

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30

Tada, Masahito, Yoshihiro Kobashigawa, Mineyuki Mizuguchi та ін. "Stabilization of Protein by Replacement of a Fluctuating Loop: Structural Analysis of a Chimera of Bovine α-Lactalbumin and Equine Lysozyme†". Biochemistry 41, № 46 (2002): 13807–13. http://dx.doi.org/10.1021/bi020360u.

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31

Katila, T., T. F. Lock, W. E. Hoffmann, and A. R. Smith. "Lysozyme, alkaline phosphatase and neutrophils in uterine secretions of mares with differing resistance to endometritis." Theriogenology 33, no. 3 (1990): 723–32. http://dx.doi.org/10.1016/0093-691x(90)90549-9.

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32

Mališauskas, Mantas, Vladimir Zamotin, Jana Jass, Wim Noppe, Christopher M. Dobson, and Ludmilla A. Morozova-Roche. "Amyloid Protofilaments from the Calcium-binding Protein Equine Lysozyme: Formation of Ring and Linear Structures Depends on pH and Metal Ion Concentration." Journal of Molecular Biology 330, no. 4 (2003): 879–90. http://dx.doi.org/10.1016/s0022-2836(03)00551-5.

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33

Abhishek, Mishra Asha Yadav Shardhanjali Behera. "Antimicrobial peptides from domestic & farm animals and its uses in veterinary medicine." Vet Farm Frontier 02, no. 04 (2025): 40–43. https://doi.org/10.5281/zenodo.15362986.

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Antimicrobial peptides (AMPs) are naturally occurring substances vital to the innate immune response against various pathogens. Over 4000 AMPs have been identified, with around 3000 sequences cataloged in databases, predominantly derived from animals and plants. They exhibit broad-spectrum antimicrobial activity, classified based on their source, composition, and activity, including antibacterial, antifungal, antiviral, antiparasitic, and antitumor properties. AMPs can be synthesized either constitutively or in response to pathogens, interacting with microbial membranes to compr

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34

Marth, Christina D., Simon M. Firestone, Dave Hanlon, et al. "Innate immune genes in persistent mating-induced endometritis in horses." Reproduction, Fertility and Development 30, no. 3 (2018): 533. http://dx.doi.org/10.1071/rd17157.

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Persistent mating-induced endometritis (PMIE) severely decreases fertility in horses. The aim of the present study was to evaluate differences between horses susceptible to PMIE and a control group in terms of the expression of selected immune response and effector genes, and the effects of oestrous cycle stage on this expression. Endometrial biopsies from 18 uterine samples of mares in the control group (eight in dioestrus, 10 in oestrus) and 16 PMIE-susceptible mares (four in dioestrus, 12 in oestrus) were analysed by quantitative real-time reverse transcription–polymerase chain reaction. Ge

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35

Haezebrouck, P., L. Morozova, and F. Van Cauwelaert. "The thermal stability of equine and pigeon lysozymes." Journal of Inorganic Biochemistry 43, no. 2-3 (1991): 395. http://dx.doi.org/10.1016/0162-0134(91)84380-r.

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36

Aramini, James M., Toshifumi Hiraoki, Yue Ke, Katsutoshi Nitta, and Hans J. Vogel. "Cadmium-113 NMR Studies of Bovine and Human a-Lactalbumin and Equine Lysozyme1." Journal of Biochemistry 117, no. 3 (1995): 623–28. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a124754.

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37

Malisauskas, Mantas, Johan Ostman, Adas Darinskas, et al. "Does the Cytotoxic Effect of Transient Amyloid Oligomers from Common Equine Lysozymein VitroImply Innate Amyloid Toxicity?" Journal of Biological Chemistry 280, no. 8 (2004): 6269–75. http://dx.doi.org/10.1074/jbc.m407273200.

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38

Ragona, Giuseppe, Franco Corrias, Martina Benedetti, et al. "Amiata donkey milk chain: animal health evaluation and milk quality." Italian Journal of Food Safety 5, no. 3 (2016). http://dx.doi.org/10.4081/ijfs.2016.5951.

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This study presents an investigation of Amiata donkey health and quality of milk for human consumption. Thirty-one lactating dairy jennies were examined. The following samples were collected: faecal samples from the rectum of animals for parasitological examination; cervical swabs for the detection of bacteria causing reproductive disorders; and blood samples for serological diagnosis of main zoonotic (<em>Brucella</em> spp., <em>Leptospira</em> spp.) and donkey abortion agents (<em>Brucella</em> spp., <em>Leptospira</em> spp., <em>Salmonel

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39

Moroni, Rebecca, Diana Fanelli, Francesco Camillo, et al. "Endometrial expression of antimicrobial peptides as markers of subclinical endometritis in mares." Equine Veterinary Journal, March 2, 2024. http://dx.doi.org/10.1111/evj.14080.

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AbstractBackgroundEndometritis is a major cause of subfertility in mares. Multiparous old mares are more susceptible to developing endometritis given that ageing is associated with an altered immune response and with inadequate physiological uterine clearance after breeding, which can lead to degenerative changes in the endometrium. Molecules such as antimicrobial peptides (AMPs) have been proposed as endometritis markers in the equine species.Study designCross‐sectional.ObjectivesTo investigate the endometrial expression of defensin‐beta 4B (DEFB4B), lysozyme (LYZ) and secretory leukocyte pep

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