title: Purification of lysozyme from other hen's-egg-white proteins using metal-affinity precipitation.
abstract: It was found that the presence of 5 mM Cu(2+) caused precipitation of protein present in hen's egg white to a large extent. About 85% of lysozyme activity remained in the supernatant and the enzyme was purified by approx. 13-fold. A further gel-filtration step on Sephadex G-75 resulted in an overall yield of 80% for the enzyme with 655-fold purification, and showed a single band on SDS/PAGE.
authors.affiliation: Chemistry Department, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India.
authors.forename: Ipsita
authors.initials: I
authors.lastname: Roy
authors.forename: Mukkavilli V S
authors.initials: MV
authors.lastname: Rao
authors.forename: Munishwar N
authors.initials: MN
authors.lastname: Gupta
mesh_terms: D000345:Affinity Labels / Q000737:chemistry; D000818:Animals; D011232:Chemical Precipitation; D002645:Chickens; D002846:Chromatography, Affinity / Q000379:methods*; D003300:Copper / Q000737:chemistry*; D004527:Egg Proteins / Q000737:chemistry / Q000302:isolation & purification*; D004789:Enzyme Activation; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: D000345:Affinity Labels; D004527:Egg Proteins; D003300:Copper; D009113:Muramidase