Alcantara J, Padda J S, Schryvers A B
Department of Microbiology and Infectious Diseases, University of Calgary, Alta., Canada.
Can J Microbiol. 1992 Nov;38(11):1202-5. doi: 10.1139/m92-198.
The oligosaccharides of human lactoferrin were enzymatically removed with glycopeptidase F, resulting in a preparation containing partial and fully deglycosylated human lactoferrin. The derivatives were separated by Concanavalin A affinity chromatography and compared with native human lactoferrin with respect to their ability to bind to bacterial receptors. Competitive binding experiments demonstrated that the lactoferrin derivatives were equally capable as native lactoferrin in binding to receptors of Neisseria meningitidis, Neisseria gonorrhoeae, and Moraxella catarrhalis. This result indicates that the oligosaccharides on human lactoferrin are not essential for binding to the bacterial receptors.
人乳铁蛋白的寡糖用糖肽酶F酶解去除，得到一种含有部分和完全去糖基化人乳铁蛋白的制剂。通过伴刀豆球蛋白A亲和色谱法分离这些衍生物，并就其与细菌受体结合的能力与天然人乳铁蛋白进行比较。竞争性结合实验表明，乳铁蛋白衍生物与天然乳铁蛋白在结合脑膜炎奈瑟菌、淋病奈瑟菌和卡他莫拉菌的受体方面具有同等能力。这一结果表明，人乳铁蛋白上的寡糖对于与细菌受体的结合并非必不可少。
