Linked Life Data

2112461

Source:http://linkedlifedata.com/resource/pubmed/id/2112461

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-7-13
pubmed:abstractText
Glycosylation can affect the physical and biochemical properties of the polypeptide chain in glycoproteins. Asparagine-N-linked polylactosaminyl glycosylation of the chymotryptic 44-kDa gelatin-binding domain from human placental fibronectin confers protease resistance [Zhu, B. C. R., Fisher, S. F., Panda, H., Calaycay, J., Shively, J. E. & Laine, R. A. (1984) J. Biol. Chem. 259, 3962-3970] and weaken the binding to gelatin [Zhu, B. C. R. & Laine, R. A. (1985) J. Biol. Chem. 260, 4041-4045]. Intrinsic tryptophan fluorescence of the gelatin-binding domain was used to probe glycosylation-dependent protein conformation changes. In gelatin-binding fragments containing incrementally smaller polylactosamine oligosaccharides, the fluorescence intensity progressively decreased and the emission spectrum shifted about 7 nm to the blue. Removal of the polylactosamine chains from a highly glycosylated fragment with endo-beta-galactosidase from Escherichia freundii also quenched the protein fluorescence. The fluorescence lifetimes did not appear to be affected by the extent of glycosylation, suggesting static quenching of the tryptophan emission in the low glycosylated fragments. Acrylamide quenching studies showed that the accessibility of the tryptophans to small solutes was not altered by glycosylation. The steady-state emission anisotropy increased with decreasing polylactosamine chain length. The results indicate that the polylactosamine chains alter the tryptophan environments in the gelatin-binding domain, probably by changing the polypeptide conformation. These putative protein conformation changes may be partially responsible for the altered gelatin binding, protease resistance, and cell adhesion functions of fetal tissue fibronectin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
189
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
509-16
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2112461-Acrylamide, pubmed-meshheading:2112461-Acrylamides, pubmed-meshheading:2112461-Amino Sugars, pubmed-meshheading:2112461-Binding Sites, pubmed-meshheading:2112461-Chymotrypsin, pubmed-meshheading:2112461-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2112461-Female, pubmed-meshheading:2112461-Fibronectins, pubmed-meshheading:2112461-Gelatin, pubmed-meshheading:2112461-Glycoproteins, pubmed-meshheading:2112461-Glycoside Hydrolases, pubmed-meshheading:2112461-Glycosylation, pubmed-meshheading:2112461-Humans, pubmed-meshheading:2112461-Mathematics, pubmed-meshheading:2112461-Placenta, pubmed-meshheading:2112461-Protein Conformation, pubmed-meshheading:2112461-Spectrometry, Fluorescence, pubmed-meshheading:2112461-Tryptophan, pubmed-meshheading:2112461-beta-Galactosidase
pubmed:year
1990
pubmed:articleTitle
Intrinsic tryptophan fluorescence measurements suggest that polylactosaminyl glycosylation affects the protein conformation of the gelatin-binding domain from human placental fibronectin.
pubmed:affiliation
Department of Biochemistry, Louisiana State University, Baton Rouge 70803.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.