Linked Life Data

16546339

Source:http://linkedlifedata.com/resource/pubmed/id/16546339

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-5-16
pubmed:abstractText
A sensitive, accurate, and efficient biosensor analysis using surface plasmon resonance (SPR) spectroscopy was used for delineating the molecular interaction between rabbit liver asialoglycoprotein receptors (ASGPR) and glycosylated proteins. Isolated rabbit liver ASGPR obtained by affinity column chromatography was dissolved in buffer solution containing TritonX-100 and immobilized on the SPR sensor chip by amine coupling. The SPR study demonstrated that the association rate constants (ka) of galactosylated proteins with ASGPR are dependent on the number of galactose residues, while the dissociation rate constants (kd) are influenced not only by the surface density of the galactose moieties but also by their steric configuration. In addition, it was demonstrated that D-fucosylated BSA had a higher binding affinity to ASGPR than Gal-BSA, when the degree of sugar modification was equivalent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0731-7085
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
966-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Analysis of the molecular interaction of glycosylated proteins with rabbit liver asialoglycoprotein receptors using surface plasmon resonance spectroscopy.
pubmed:affiliation
Department of Drug Delivery Research, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't