Linked Life Data

11926987

Source:http://linkedlifedata.com/resource/pubmed/id/11926987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-4-2
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
511-5
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
N-glycans stabilize human erythropoietin through hydrophobic interactions with the hydrophobic protein surface: studies by surface plasmon resonance analysis.
pubmed:affiliation
Course of Applied Biochemistry, Graduate School of Agriculture and Biological Science, Osaka Prefecture University, Sakai, 599-8531, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't