PMID: 11926987Apr 3, 2002Paper

N-glycans stabilize human erythropoietin through hydrophobic interactions with the hydrophobic protein surface: studies by surface plasmon resonance analysis

Journal of Biochemistry
Teruko ToyodaHaruki Yamaguchi

Abstract

Human erythropoietin (EPO) produced in Chinese hamster ovary cells is a hydrophobic protein highly stabilized by multibranched complex-type N-glycans. To reveal the molecular basis of the interaction between the N-glycans and the EPO protein, complex-type N-glycans of different structures were analyzed as to their binding affinity for Escherichia coli-expressed EPO by means of the surface plasmon resonance technique. It appears well established that complex-type N-glycans, particularly multibranched ones, have hydrophobic regions that extensively stretch across the plane holding acetylamino groups and that N-glycan-protein hydrophobic interactions characterized by a slow rate of dissociation stabilize the protein conformation.

Citations

Mar 4, 2011·Proceedings of the National Academy of Sciences of the United States of America·Zhongping TanSamuel J Danishefsky
Sep 22, 2009·The Journal of Biological Chemistry·John F Valliere-DouglassAlain Balland
Jul 28, 2010·Protein Science : a Publication of the Protein Society·Lynn ZieglerDaniel J Kosman
Apr 25, 2012·Journal of the American Chemical Society·Christopher R EllisWilliam G Noid
Jan 21, 2004·Journal of Molecular Recognition : JMR·Rebecca L Rich, David G Myszka
Jul 29, 2009·Biotechnology Progress·Yan LiuShaoqiu Zhuo
Nov 20, 2016·The Journal of Pharmacy and Pharmacology·Brittney J Mills, Jennifer S Laurence Chadwick
Dec 1, 2017·The Journal of Biological Chemistry·Elisabeth GludovaczThomas Boehm

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