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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2000-12-20
pubmed:abstractText
Binding of allergen-IgE complexes to the high affinity IgE receptor (Fc epsilonRI) on mast cells and basophils leads to the release of various mediaters such as histamine. Fab fragments prepared by the papain digestion of humanized antibody against human Fc epsilonRI inhibited the release of histamine from human basophils. Here we established an expression system to directly produce Fab fragments of the humanized anti-human Fc epsilonRI antibody in methylotropic yeast, P. pastoris. Fab fragments were efficiently secreted into the medium at a concentration of 10-40 mg/L using a signal sequence from the P. pastoris phosphatase gene. They were consisted of disulfide-linked light and heavy chains correctly starting from the first amino acid residues by proper cleavage of the signal peptides. The obtained Fab fragments inhibited the binding between IgE and Fc epsilonRI as efficiently as the counterpart prepared by papain digestion of the whole antibody.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2138-44
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Production of humanized Fab fragment against human high affinity IgE receptor in Pichia pastoris.
pubmed:affiliation
Foods & Pharmaceuticals Research & Development Laboratory, Asahi Breweries Ltd., Kitasoma-gun, Ibaraki, Japan. kyoko.takahashi@asahibeer.co.jp
pubmed:publicationType
Journal Article