Linked Life Data

9278288

Source:http://linkedlifedata.com/resource/pubmed/id/9278288

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-10-10
pubmed:databankReference
pubmed:abstractText
We have designed and expressed bivalent small immune proteins (SIP) based on scFv fragments connected through a short linker of four amino acids to the CH3 domain of the human immunoglobulin gamma 1 H-chain. Three different versions have been designed and expressed in mammalian cells. In one construct a cysteine residue was included in the last amino acid of the flexible 15-amino acid long linker connecting the V(L) and V(H) domains, thus creating a disulphide bond stabilized molecule. A version with a shorter (five amino acids) V(L)/V(H) linker was also produced and shown to be efficiently assembled and secreted. All three SIPs form dimers retaining their antigenic specificity in Western blotting and having a comparable functional affinity (avidity) as determined by ELISA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
731-6
pubmed:dateRevised
2006-4-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Mammalian cell expression of dimeric small immune proteins (SIP).
pubmed:affiliation
International Centre for Genetic Engineering and Biotechnology, Area Science Park, Trieste, Italy.
pubmed:publicationType
Journal Article