title: Detection of a glycosylated form of hen egg white lysozyme.
abstract: By assaying lysozyme activity after denaturing polyacrylamide gel electrophoresis of commercial hen egg white lysozyme preparations, minor lysozymal activity was detected as an 18-kDa protein. After electrophoretic purification for microsequencing, the N-terminus sequence of the 18-kDa lysozyme was found to be identical with mature 14.4-kDa hen egg white lysozyme. The 18-KDa hen egg white lysozyme was judged to be glycosylated based on 3.6-kDa decrease in molecular mass after N-glycosidase F treatment, binding to concanavalin A-Sepharose, and staining with periodate-Schiff's reagent. The minor form corresponded to about 0.3% of lysozyme molecules.
authors.affiliation: Département de phytologie, Faculté des sciences de l'agriculture et de l'alimentation, Université Laval, QC, Canada.
authors.forename: J
authors.initials: J
authors.lastname: Trudel
authors.forename: A
authors.initials: A
authors.lastname: Asselin
mesh_terms: D000818:Animals; D002645:Chickens; D004527:Egg Proteins / Q000378:metabolism*; D006031:Glycosylation; D009113:Muramidase / Q000378:metabolism*
chemical_list: D004527:Egg Proteins; D009113:Muramidase