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The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis.
van Veen HA, Geerts ME, van Berkel PH, Nuijens JH. van Veen HA, et al. Eur J Biochem. 2004 Feb;271(4):678-84. doi: 10.1111/j.1432-1033.2003.03965.x. Eur J Biochem. 2004. PMID: 14764083 Free article.
Apparently, the previously reported protection by N-linked glycosylation of hLF [van Berkel, P.H.C., Geerts, M.E.J., van Veen, H.A., Kooiman, P.M., Pieper, F., de Boer, H.A. & Nuijens, J.H. (1995) Biochem. ...
Apparently, the previously reported protection by N-linked glycosylation of hLF [van Berkel, P.H.C., Geerts, M.E.J., van Veen, …
Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis.
van Berkel PH, Geerts ME, van Veen HA, Kooiman PM, Pieper FR, de Boer HA, Nuijens JH. van Berkel PH, et al. Among authors: geerts me. Biochem J. 1995 Nov 15;312 ( Pt 1)(Pt 1):107-14. doi: 10.1042/bj3120107. Biochem J. 1995. PMID: 7492299 Free PMC article.
159 results