Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-2-28
pubmed:databankReference
pubmed:abstractText
The potential of recombinant antibody fragments is likely to be fulfilled only if they can be produced routinely at high concentrations. We have compared the ability of Escherichia coli and Pichia pastoris to produce functional recombinant single chain antibody (scAb) fragments. Two scAb fragments were expressed, an antihuman type V acid phosphatase (TRAP) and an anti-Pseudomonas aeruginosa lipoprotein I. We report here that, while expression from P. pastoris resulted in a significantly increased level of expression of the anti-TRAP scAb compared to E. coli, neither fragment was able to bind its target antigen as well as the bacterial product.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0266-8254
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10664964-Acid Phosphatase, pubmed-meshheading:10664964-Antigen-Antibody Reactions, pubmed-meshheading:10664964-Antigens, pubmed-meshheading:10664964-Bacterial Proteins, pubmed-meshheading:10664964-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:10664964-Escherichia coli, pubmed-meshheading:10664964-Genes, Immunoglobulin, pubmed-meshheading:10664964-Immunoglobulin Fragments, pubmed-meshheading:10664964-Immunoglobulin Heavy Chains, pubmed-meshheading:10664964-Immunoglobulin Variable Region, pubmed-meshheading:10664964-Immunoglobulin kappa-Chains, pubmed-meshheading:10664964-Lipoproteins, pubmed-meshheading:10664964-Molecular Sequence Data, pubmed-meshheading:10664964-Pichia, pubmed-meshheading:10664964-Recombinant Proteins, pubmed-meshheading:10664964-Transformation, Bacterial, pubmed-meshheading:10664964-Transformation, Genetic
pubmed:year
1999
pubmed:articleTitle
Cloning and expression of single chain antibody fragments in Escherichia coli and Pichia pastoris.
pubmed:affiliation
Department of Molecular and Cell Biology, University of Aberdeen, Scotland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't