Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1991-12-26
pubmed:abstractText
Recombinant human thyroid peroxidase (hTPO) has been expressed in eukaryotic cells as both the membrane-associated enzyme and as a secreted protein. We now report overexpression of the secreted form of recombinant hTPO in eukaryotic cells. For hTPO gene amplification we used a vector containing the mouse dihydrofolate reductase (DHFR) gene. Stably transfected Chinese hamster ovary (CHO) cells were grown in the presence of increasing concentrations of methotrexate (MTX) and hTPO expression was measured immunologically in an enzyme-linked immunosorbent assay (ELISA). Progressive overexpression of secreted hTPO occurred up to a final MTX concentration of 10,000 nM. Slot-blot analysis of genomic DNA from CHO cells expressing truncated hTPO revealed amplification profiles of the DHFR and hTPO genes to be similar, in parallel with hTPO protein production. High-level expression of secreted hTPO offers the potential for obtaining large amounts of biologically and immunologically active protein for future study.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-14
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Overexpression of an immunologically-intact, secreted form of human thyroid peroxidase in eukaryotic cells.
pubmed:affiliation
Thyroid Molecular Biology Unit, V.A. Medical Center, San Francisco, CA 94121.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.