Biological Properties of a Recombinant Human Immunoglobulin ε -Chain Fragment

Teruko Ishizaka; Birgit Helm; John Hakimi; Jennifer Niebyl; Kimishige Ishizaka; Hannah Gould

doi:10.1073/pnas.83.21.8323

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Biological Properties of a Recombinant Human Immunoglobulin ε -Chain Fragment

Journal article

Open access

Peer reviewed

Biological Properties of a Recombinant Human Immunoglobulin ε -Chain Fragment

Teruko Ishizaka, Birgit Helm, John Hakimi, Jennifer Niebyl, Kimishige Ishizaka and Hannah Gould

Proceedings of the National Academy of Sciences of the United States of America, Vol.83(21), pp.8323-8327

11/01/1986

DOI: 10.1073/pnas.83.21.8323

PMCID: PMC386920

PMID: 2430285

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Abstract

A recombinant human immunoglobulin ε -chain gene expression product (rFc ) was compared with a human E myeloma protein in the affinity for ε -chain Fc fragment receptors (Fc R) on cultured human basophils. The association-dissociation kinetics of the rFc -Fc R interaction are indistinguishable from that of E myeloma protein, indicating that rFc and IgE have identical affinity for the receptors. The recombinant gene product sensitizes cultured basophils for anti-IgE-induced histamine release. A dose-response curve of histamine release indicates that the gene product is equally efficient in transducing the signal for degranulation as the natural IgE. Both the rFc and IgE lost the affinity for Fc R by heating at 56 degrees C. Upon renaturation by passage through a solution of 6 M guanidine hydrochloride, rFc recovered both the affinity for Fc R and the original CD spectra. On the other hand, renaturation of heat-denatured IgE largely restored optical activity above 250 nm but restored neither the affinity for Fc R nor the CD spectrum below 220 nm. The results suggest that either the amino acid sequence or the carbohydrate present in the myeloma protein, but not the rFc , may interfere with refolding of the receptor-binding structures.

Antibodies

Immunology

Ligands

Receptors

T lymphocytes

Molecules

Basophils

Cultured cells

Histamines

Histamine release

Details

Title: Subtitle: Biological Properties of a Recombinant Human Immunoglobulin ε -Chain Fragment
Creators: Teruko Ishizaka
Birgit Helm
John Hakimi
Jennifer Niebyl - University of Iowa, Obstetrics and Gynecology
Kimishige Ishizaka
Hannah Gould
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences of the United States of America, Vol.83(21), pp.8323-8327
DOI: 10.1073/pnas.83.21.8323
PMID: 2430285
PMCID: PMC386920
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences of the United States of America
Language: English
Date published: 11/01/1986
Academic Unit: Obstetrics and Gynecology
Record Identifier: 9983557241402771

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