Linked Life Data

2532539

Source:http://linkedlifedata.com/resource/pubmed/id/2532539

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1990-2-15
pubmed:abstractText
An assay for UDP-Glc:glycoprotein glucosyltransferase was developed. Incubation of rat liver microsomes with UDP-[14C]Glc led to the formation of hot trichloroacetic acid insoluble material identified as protein-linked Glc1Man7-9GlcNAc2. Addition of 8 M urea-denatured thyroglobulin to the incubation mixtures stimulated up to 10-12-fold the formation of the same compounds but only in the presence of detergents. Native thyroglobulin was ineffective. Several experiments indicated that the stimulation was due to the transfer of glucose residues from UDP-Glc to high-mannose oligosaccharides in urea-denatured thyroglobulin and that this transfer reaction did not involve dolichol mono- or diphosphate derivatives as intermediates. The glycoprotein glucosylating activity was mainly located in the endoplasmic reticulum and could glucosylate glycopeptides derived from the digestion of thyroglobulin with an unspecific protease. Glucosylation of oligosaccharides in those glycopeptides occurred, however, at a rate at least 2 orders of magnitude slower than that of the same compounds in urea-denatured thyroglobulin. Tryptic digestion of urea-denatured thyroglobulin did not affect its glucosylation rate. The structure of Glc1Man9GlcNAc2 linked to urea-denatured thyroglobulin was identical with that of Glc1Man9GlcNAc2-P-P-dolichol. The assay of UDP-Glc:glycoprotein glucosyltransferase allowed detection of the activity in microsomal membranes in which endogenous acceptors appeared to be absent or almost absent, such as those derived from mung bean, Mucor rouxii, Crithidia fasciculata, and Trypanosoma cruzi cells.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8108-16
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:2532539-Acetylglucosaminidase, pubmed-meshheading:2532539-Animals, pubmed-meshheading:2532539-Crithidia, pubmed-meshheading:2532539-Glucose, pubmed-meshheading:2532539-Glucosyltransferases, pubmed-meshheading:2532539-Glycoproteins, pubmed-meshheading:2532539-Glycosylation, pubmed-meshheading:2532539-Hexosyltransferases, pubmed-meshheading:2532539-Male, pubmed-meshheading:2532539-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, pubmed-meshheading:2532539-Membrane Proteins, pubmed-meshheading:2532539-Microsomes, pubmed-meshheading:2532539-Microsomes, Liver, pubmed-meshheading:2532539-Mucor, pubmed-meshheading:2532539-Peptide Hydrolases, pubmed-meshheading:2532539-Plants, pubmed-meshheading:2532539-Protein Denaturation, pubmed-meshheading:2532539-Rats, pubmed-meshheading:2532539-Saccharomyces cerevisiae, pubmed-meshheading:2532539-Streptomyces griseus, pubmed-meshheading:2532539-Subcellular Fractions, pubmed-meshheading:2532539-Transferases, pubmed-meshheading:2532539-Trypanosoma cruzi
pubmed:year
1989
pubmed:articleTitle
Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes.
pubmed:affiliation
Instituto de Investigaciones Bioquímicas Fundación Campomar, IIB-FCEN-UBA, IIBBA-CONICET, Buenos Aires, Argentina.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't