The receptor for immunoglobulin E: Examination for kinase activity and as a substrate for kinases

Rodolfo Quarto, Henry Metzger

Research output: Contribution to journalArticle

Abstract

Purified receptor-immunoglobulin E (IgE) complexes incubated with [γ-32P]-ATP incorporated phosphorus into tryosines on the β and γ chains of the receptor. The activity had the typical characteristics of a tyrosine kinase. Immunoprecipitation of the complexes with anti-IgE left the activity in the supernatant, demonstrating that the receptor itself was not the kinase. The receptor was also phosphorylated when membranes or intact cells were incubated with radioactive ATP or phosphate, respectively, but in each case the subunits or amino acid residues that were modified were distinctive.

Original languageEnglish
Pages (from-to)1215-1223
Number of pages9
JournalMolecular Immunology
Volume23
Issue number11
DOIs
Publication statusPublished - 1986

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IgE Receptors
Phosphotransferases
Adenosine Triphosphate
Immunoprecipitation
Protein-Tyrosine Kinases
Phosphorus
Immunoglobulin E
Phosphates
Amino Acids
Membranes

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

The receptor for immunoglobulin E : Examination for kinase activity and as a substrate for kinases. / Quarto, Rodolfo; Metzger, Henry.

In: Molecular Immunology, Vol. 23, No. 11, 1986, p. 1215-1223.

Research output: Contribution to journalArticle

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