Biochemical Isolation and Characterization of Hyaluronidase Enzyme from Venom of Egyptian Honey Bee Apis Mellifera Lamarckii
References
- Baumgartner, G. (1998). The impact of extracellular matrix on chemoresistance of solid tumors-experimental and clinical results of hyaluronidase as additive to cytostatic chemotherapy. Cancer Letters, 131(1), 85–99.
- Bordon, K. C., Wierel, G. A., Amorim, F. G., & Arantes, E. C. (2015). Arthropod venom hyaluronidases biochemical properties and potential applications in medicine and biotechnology. Journal of venomous Animals and Toxins including Tropical Diseases, 22, 21, 43. DOI: 10.1186/s40409-015-0042-7
- Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.
- Farr, C., Menzel, J., Seeberger, J., & Schweigle, B. (1997). Clinical pharmacology and possible applications of hyaluronidase with reference to Hylase “Dessau”. Wiener Medizinische Wochenschrift, 147, 347–355.
- Girish, K. S., Mohankumari, H. P., Nagaraju, S., Vishwanath, B. S., Kemparaju, K. (2004). Hyaluronidase and protease activities from Indian snake venoms: neutralization by Mimosa pudica root extract. Fitoterapia, 75(3–4), 378–380. DOI: 10.1016/j.fitote.2004.01.006
- Gmachl, M. & Kreil, G. (1993). Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Proceedings of the National Academy of Sciences. USA, 90, 3569–3573.
- Guntenhöner, M. W., Pogrel, M. A., & Stem, R. (1992). A substrate-gel assay for hyaluronidase activity. Matrix, 12(5), 388–396. DOI: 10.1016/s0934-8832(11)80035-1
- Justo Jacomini, D. L., Campos Pereira, F. D., Aparecido dos Santos Pinto, J. R., dos Santos, L. D., da Silva Neto, A. J., Giratto, D.T., … Brochetto Braga, M. R. (2013). Hyaluronidase from the venom of the social wasp Polybia paulista (Hymenoptera, Vespidae): Cloning, structural modeling, purification, and immunological analysis. Toxicon, 15(64), 70–80. DOI: 10.1016/j.toxicon.2012.12.019
- Kemeny, D. M, Dalton, N., Lawrence, A. J., Pearce, F. L., Vernon, C. A. (1984). The purification and characterisation of hyaluronidase from the venom of the honey bee, Apis mellifera. European Journal of Biochemistry, 139(2), 217–23. DOI: 10.1111/j.1432-1033.1984.tb07997
- Kemparaju, K., & Girish, K. S. (2006). Snake venom hyaluronidase: a therapeutic target. Cell Biochemistry and Function, 24, 7–12. DOI: 10.1002/cbf.1261
- Klocker, J., Sabitzer, H., Raunik, W., Wieser, S., & Schumer, J. (1995). Combined application of cisplatin, vindesine, hyaluronidase and radiation for treatment of advanced squamous cell carcinoma of the head and neck. American Journal of Clinical Oncology, 18(5), 425–428. DOI: 10.1097/00000421-199510000-00013
- Kokot, Z. J., Matysiak, J., Kłos, J., Kędzia, B., & Hołderna-Kędzia, E. (2009). Application of Principal Component Analysis for evaluation of chemical and antimicrobial properties of honey bee (Apis mellifera) venom. Journal of Apicultural Research, 48(3), 168–175. DOI: 10.3896/IBRA.1.48.3.04
- Kolarich, D., Leonard, R., Hemmer, W., & Altmann, F. (2005). The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its isoform in Vespula vulgaris. FEBS Journal, 272(20), 5182–5190. DOI: 10.1111/j.1742-4658.2005.04841.x
- Krylov, V. N. (1995): Bee venom. Properties, receipt, use: Novgorod, 224.
- Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature, 227, 680–685.
- Makris, G., Wright, J. D., Ingham, E. I., & Holland, K. T. (2004). The hyaluronate lyase of Staphylococcus aureus - a virulence factor? Microbiology, 150(6), 2005–2013. DOI: 10.1099/mic.0.26942-0
- Maksimenko, A. V., Petrova, M. L., Tischenko, E. G., & Schechilina, Y. V. (2001). Chemical modification of hyaluronidase regulates its inhibition by heparin. European Journal of Pharmaceutics and Biopharmaceutics, 51(1), 33–38. DOI: 10.1016/s0939-6411(00)00136-3
- Matsushita, O., & Okabe, A. (2001). Clostridial hydrolytic enzymes degrading extracellular components. Toxicon, 39(11), 1769–1780. DOI: 10.1016/s0041-0101(01)00163-5
- Moga, M. A, Dimienescu, O. G., Arvătescu, C. A., Ifteni, P., Pleş, L. (2018). Anticancer Activity of Toxins from Bee and Snake Venom- An Overview on Ovarian Cancer. Molecules, 23(3), 692–713. DOI: 10.3390/molecules23030692
- Morey, S. S., Kiran, K. M., & Gadag, J. R. (2006). Purification and properties of hyaluronidase from Palamneus gravimanus (Indian black scorpion) venom, Toxicon, 47(2), 188–95. DOI: 10.1016/j.toxicon.2005.10.014
- Muckenschnabel, I., Bernhardt, G., Spruss, T., & Buschauer, A. (1996). Hyaluronidase pretreatment produces selective melphalan enrichment in malignant melanoma in nude mice. Cancer Chemotherapy and Pharmacology, 38(1), 88–94. DOI: 10.1007/s002800050452
- Nagaraju, S., Devaraja, S., & Kemparaju, K. (2007). Purification and properties of hyaluronidase from Hippasa partita (funnel web spider) venom gland extract. Toxicon, 50(3), 383–393. DOI: 10.1016/j.toxicon.2007.04.007
- O’Farrell, P. H. (1975). High resolution two-dimentional electrophoresis of proteins. Journal of Biological Chemistry, 25(10), 4007–4021.
- Pukrittayakamee, S., Warrel, D.A., Deasakorn, V., Mc Michael, A.J., White, N.J., Bunnag, G.D. (1988). The hyaluronidase activities of some Southeast Asian snake venoms. Toxicon, 26(7), 629–637. DOI: 10.1016/0041-0101(88)90245-0
- Senff-Ribeiro, A., Henrique Da Silva, P., Chaim, O.M., Gremski, L.H., Paludo, K.S., Bertoni Da Silveira, R., … Veiga, S.S. (2008). Biotechnological applications of brown spider (Loxosceles genus) venom toxins. Biotechnology Advances, 26(3), 210–218. DOI: 10.1016/j.biotechadv.2007.12.003
- Smith, I. (1969). Acrylamide gel disc electrophoresis. In “Electrophoretic techniques” (Edited by Smith, I.) pp. 365–515, Academic press, New York.
- Sutti, R., Tamascia, M. L., Hyslop, S., & Rocha-E-Silva, T. A. (2014). Purification and characterization of a hyaluronidase from venom of the spider Vitalius dubius (Araneae, Theraphosidae). Journal of Venomous Animals and Toxins including Tropical Diseases, 20(2), 1–7. DOI: 10.1186/1678-9199-20-2
- Topchiyeva, A. & Mammadova F. Z. (2016). The seasonal activity of hyaluronidase in venom of a honey bee (Apis mellifera L. caucasica) in various regions of Azerbaijan. Journal of Entomology and Zoology Studies, 4(4), 1388–1391.
- Wahby, A. F., Mahdy, el-SM., El-Mezayen, H. A., Salama, W. H., Abdel-Aty, A. M., Fahmy, A. S. (2012). Egyptian horned viper Cerastes cerastes venom hyaluronidase: Purification, partial characterization and evidence for its action as a spreading factor. Toxicon, 60(8), 1380–1389. DOI: 10.1016/j.toxicon.2012.08.016
- Weber, K., & Osborn, M. (1969). The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry, 244(16), 4406–4412.
- Wehbe, R., Frangieh, J., Rima, M., El Obeid, D., Sabatier, J., Fajloun, Z. (2019). Bee venom: overview of main compounds and bioactivities for therapeutic interests. Molecules, 24, 2997. DOI: 10.3390/molecules24162997
- Zahalka, M. A., Okon, E., Gosslar, U., Holzmann, B., Naor, D. (1995). Lymph node (but not spleen) invasion by murine lymphoma is both CD44- and hyaluronate-dependent. Journal of Immunology, 154(10), 5345–5355.
- Zheng, Y., Deng, X., Zhao, Y., & Martin-DeLeon, P.A. (2001). SPAM1 (PH-20) mutations and sperm dysfunction in mice with the Rb (6.16) or Rb (6.15) translocation. Mammalian Genome, 12(11), 822–829. DOI: 10.1007/s00335-001-1008-3
DOI: https://doi.org/10.2478/jas-2020-0015 | Journal eISSN: 2299-4831 | Journal ISSN: 1643-4439 (formerly 2299-4831)
Language: English
Page range: 153 - 164
Submitted on: Dec 4, 2019
Accepted on: Mar 3, 2020
Published on: Jul 2, 2020
Published by: The National Institute of Horticultural Research and Apicultural Research Association
In partnership with: Paradigm Publishing Services
Keywords:
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© 2020 Mohammed M. Abdel-Monsef, Hind A. Zidan, Doaa A. Darwish, Hassan M. Masoud, Mohamed S. Helmy, Mahmoud A. Ibrahim, published by The National Institute of Horticultural Research and Apicultural Research Association
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.