Linked Life Data

1627179

Source:http://linkedlifedata.com/resource/pubmed/id/1627179

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-8-13
pubmed:abstractText
Asexual blood forms of the human malaria parasite, Plasmodium falciparum, synthesize a major glycosylated 195 kDa protein that has been considered for the development of a vaccine. beta-Elimination-borohydride reduction of the 195 kDa glycoprotein and its 16 kDa processed product after metabolic labeling of their carbohydrates, showed the presence of derived, labeled glucosaminitol and alanine. This suggests that the 195 and 16 kDa glycoproteins contain distinct O-glycosyl linkages and that N-acetylglucosamine and serine residues are involved in the attachment of carbohydrate moieties to the protein core. Endo-O-glycanase treatment of total glycoproteins shows that O-glycosidycally-linked sugars represent a major carbohydrate moiety in P. falciparum glycoproteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Plasmodium falciparum synthesizes O-glycosylated glycoproteins containing O-linked N-acetylglucosamine.
pubmed:affiliation
World Health Organization-Immunology Research Training Centre, Centre Médical Universitaire, Geneva, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't