Lysozyme from chicken egg white for Molecular Biology L7651.
Purification of lysozyme from egg white using ion exchange column chromatography and verification of the purity by biochemical and molecular technique was the sole aim of this experiment. Lysozyme, which is a positively charged protein, was made to bind with the cationic CM sepharose resins.Lysozyme, enzyme found in the secretions (tears) of the lacrimal glands of animals and in nasal mucus, gastric secretions, and egg white. Discovered in 1921 by Sir Alexander Fleming, lysozyme catalyzes the breakdown of certain carbohydrates found in the cell walls of certain bacteria (e.g., cocci).THE PURIFICATION AND PROPERTIES OF LYSOZYME BY KARL MEYER, RICHARD THOMPSON, JOHN W. PALMER, AND DEVORAH KHORAZO (From the Department of Ophthalmology, College of Physicians and Surgeons, Columbia University, and the Institute of Ophthalmology, Presbyterian Hospital, New York).
Lysozyme has a lower molecular mass (14.3 kDa from chicken egg white) than most other proteins, and therefore considerable purification can be achieved by simple gel-filtration, which separates proteins on the basis of size. Furthermore, the unique charge characteristics of lysozyme, which has an unusually high pI of 10.5, can also be exploited.LYSOZYME: TEARS OF HOPE Lim, Phoebe INTRODUCTION Lysozyme also called as N-Acetylmuramide glycanhydrolase or muramidase is an enzyme that catalyzes and hydrolyzes the glycosidic bond that connects N-acetylmuramic acid with the fourth carbon atom of N-acetylglucosamine they are part of the innate immune system and responsible for bacteriocidal to gram positive bacteria’s by attacking the.
Lysozyme is a relatively small enzyme. Hen egg white lysozyme consists of a single polypeptide of 129 amino acids in length with M r 14 600. From X-ray diffraction data, we can see that there is a distinct cleft in the lysozyme structure. The active site is located in this cleft.
