Linked Life Data

2522770

Source:http://linkedlifedata.com/resource/pubmed/id/2522770

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-4-25
pubmed:abstractText
N-acetylglucosaminyltransferase I (GlcNAc-TI) catalyzes the first reaction in the conversion of ASN-linked cell surface oligosaccharides from a mannose-terminating structure to more complex carbohydrate structures. The mutant Chinese hamster ovary (CHO) cell line, Lec1, is deficient in this enzyme and, therefore, shows increased sensitivity to the lectin, Concanavalin A, which binds to the mannose-terminating oligosaccharides that accumulate on Lec1 cell surface glycoproteins. Spontaneous revertants of the Lec1 phenotype have never been observed. We report here the isolation of stable revertants of Lec1 cells to the parental CHO cell lectin-resistance phenotype after DNA-mediated transformation with human DNA. Both primary and secondary transformants express varying levels of GlcNAc-TI enzyme activity which was stable even when the cells were cultured in nonselective conditions. Human alu repeat DNA sequences are present in the primary transformants, but these sequences could not be detected in the secondary transformants.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
159
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
554-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
DNA-mediated transformation of N-acetylglucosaminyltransferase I activity into an enzyme deficient cell line.
pubmed:affiliation
Department of Anatomy and Cell Biology, University of Miami School of Medicine, FL 33101.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.