Sandbox 36: Difference between revisions
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==Function== | ==Function== | ||
[[Image:Lys.gif]] | |||
==History== | ==History== | ||
Lysozyme was first discovered by Alexander Fleming during his research for medical antibiotics. When searching for any sort of bacterial inhibitor, he added a drop of mucus to a live culture. To Fleming’s surprise, it successfully killed the bacteria. | Lysozyme was first discovered by Alexander Fleming during his research for medical antibiotics. When searching for any sort of bacterial inhibitor, he added a drop of mucus to a live culture. To Fleming’s surprise, it successfully killed the bacteria. The phenomena was carefully analyzed and it was proved that lysozyme was the main active enzyme. Fleming had discovered one of the human body’s natural defenses against infection. Lysozyme could not successfully be used as an antibiotic however, because its large size inhibits transportation through cells<ref>Goodsell, D. (2000, September). Lysozyme. Retrieved from http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb9_1.html</ref>. The enzyme has been used in protein structure and function research because of its unique properties. | ||
As mentioned earlier lysosyme can be purified from hen egg-whites and crystallized quite simply. This has made the it the best object for X-Ray analysis for many years. The X-Ray beam diffraction of lysozyme crystals also has a extremely high resolution, reaching 0.94 Angstroms. | |||
Lysozyme was the first enzyme to ever have its structure solved. In 1965 David Chilton Phillips successfully solved the structure through X-Ray analysis with 2 angstrom resolution<ref>Lysozyme. (2008). Retrieved from http://lysozyme.co.uk/</ref>. Today lysozyme is still being used in research and is also commercially valuable enzyme used for many purposes, including the treatment of ulcers and infections, and as a food and drug preservative. | |||
==References== | |||
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