Menendez-Arias L, Gavilanes J G, Rodriguez R
Comp Biochem Physiol B. 1985;82(4):639-42. doi: 10.1016/0305-0491(85)90500-0.
The cysteine-containing tryptic peptides of pigeon egg-white lysozyme have been purified by reverse-phase chromatography and thin-layer chromatography and electrophoresis on cellulose plates. They contain the eight cysteine residues of the protein. The amino acid sequence of these peptides reveals the existence of 24 differences in comparison to the homologous regions in hen egg-white lysozyme, among the 53 sequenced residues. The sequence data are compared to the corresponding ones in other type c lysozymes. According to this study, the pigeon lysozyme exhibits ten substitutions not observed in any other type c lysozyme. Pigeon lysozyme is the most different type c lysozyme from birds, according to the data on primary structure.
鸽蛋清溶菌酶含半胱氨酸的胰蛋白酶肽段已通过反相色谱、薄层色谱以及在纤维素板上进行电泳得以纯化。它们包含该蛋白质的八个半胱氨酸残基。这些肽段的氨基酸序列显示，在53个已测序的残基中，与鸡蛋清溶菌酶的同源区域相比存在24个差异。将该序列数据与其他c型溶菌酶的相应数据进行了比较。根据这项研究，鸽溶菌酶呈现出在任何其他c型溶菌酶中均未观察到的十个取代。根据一级结构数据，鸽溶菌酶是鸟类中与其他c型溶菌酶差异最大的。
