Linked Life Data

7647102

Source:http://linkedlifedata.com/resource/pubmed/id/7647102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-9-22
pubmed:abstractText
In an attempt to define glycolipid functions we have prepared photoactivatable, iodinatable derivative of globoside and used it for photoaffinity labeling of human erythrocyte membranes. Lysogloboside (Gb4Sph) was prepared from globoside through deacylation in methanolic KOH followed by re-N-acetylation of galactosaminyl residue. The NH2 group of sphingosine residue in Gb4 Sph reacted with N-hydroxysuccinimidyl-4-azidosalicylic acid resulting in the formation of Gb4Sph-ASA which was purified by preparative tlc and column chromatography. It migrated on tlc as a single spot in two solvent systems, was susceptible to leech ceramide glycanase and could be radioiodinated to a specific radioactivity of about 200 Ci/mmol. Gb4Sph-[125I]ASA was incorporated into human erythrocytes in a time and concentration-dependent manner. Before photolysis 96% of the Gb4Sph-ASA could be removed with albumin but not with trypsin. After photolysis about 50% of the label was firmly bound to erythrocytes being resistant to albumin and trypsin treatment. The label was distributed between membrane proteins and lipids in about 1:2.3 ratio. Photolabeled proteins were analyzed by SDS-PAGE followed by autoradiography and immunostaining. Most of the radioactivity was detected in band 3 and its proteolytic fragments irrespective of the duration of photolysis. Photolabeling of erythrocyte lipids was demonstrated by Sephadex LH-20 column chromatography.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
1257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7647102-Anion Exchange Protein 1, Erythrocyte, pubmed-meshheading:7647102-Autoradiography, pubmed-meshheading:7647102-Chromatography, Gel, pubmed-meshheading:7647102-Chromatography, Thin Layer, pubmed-meshheading:7647102-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7647102-Erythrocyte Membrane, pubmed-meshheading:7647102-Globosides, pubmed-meshheading:7647102-Glycoside Hydrolases, pubmed-meshheading:7647102-Humans, pubmed-meshheading:7647102-Iodine Radioisotopes, pubmed-meshheading:7647102-Isotope Labeling, pubmed-meshheading:7647102-Kinetics, pubmed-meshheading:7647102-Membrane Lipids, pubmed-meshheading:7647102-Membrane Proteins, pubmed-meshheading:7647102-Molecular Structure, pubmed-meshheading:7647102-Oligosaccharides, pubmed-meshheading:7647102-Photolysis
pubmed:year
1995
pubmed:articleTitle
Photochemical labeling of human erythrocyte membranes with radioiodinatable azidosalicylic acid derivative of globoside.
pubmed:affiliation
Department of Biochemistry, Medical Center of Postgraduate Education, Warsaw, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't