Trudel J, Asselin A
Département de phytologie, Faculté des sciences de l'agriculture et de l'alimentation, Université Laval, QC, Canada.
Biochem Cell Biol. 1995 May-Jun;73(5-6):307-9. doi: 10.1139/o95-038.
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.
通过对市售鸡蛋白溶菌酶制剂进行变性聚丙烯酰胺凝胶电泳后测定溶菌酶活性，检测到一种分子量为18 kDa的蛋白具有轻微的溶菌酶活性。经电泳纯化用于微测序后，发现18 kDa溶菌酶的N端序列与成熟的14.4 kDa鸡蛋白溶菌酶相同。基于N-糖苷酶F处理后分子量降低3.6 kDa、与伴刀豆球蛋白A-琼脂糖结合以及高碘酸-席夫试剂染色，判断18 kDa鸡蛋白溶菌酶为糖基化形式。这种次要形式约占溶菌酶分子的0.3%。
