A mutational analysis of the epitopes of recombinant human H-ferritin.

doi:10.1016/0167-4838(90)90186-j

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Article

A mutational analysis of the epitopes of recombinant human H-ferritin.

Biochimica et biophysica acta - 19 Jun 1990

Arosio P, Cozzi A, Ingrassia R, Levi S, Luzzago A, Ruggeri G, Iacobello C, Santambrogio P, Albertini A

Abstract excerpt

Murine monoclonal antibodies were elicited by the recombinant human H-ferritin overexpressed in Escherichia coli. They had a specificity analogous to that of the antibodies elicited by natural human H-chain, and all of them showed low additivity in binding the recombinant ferritin. Four antibodies of each group were challenged with four H-ferritin mutants overexpressed in E. coli, altered in different accessible...

Topics

Amino Acid Sequence
Animals
Antibodies, Monoclonal
Antigen-Antibody Complex
Chickens
Epitopes
Escherichia coli
Ferritins
Humans
Liver
Macromolecular Substances

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Sequence Data

Mutation

Myocardium

Rats

Recombinant Proteins

Sequence Homology, Nucleic Acid

Source

Open in PubMed

Identifiers

PMID: 1694692
DOI: 10.1016/0167-4838(90)90186-j

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1694692-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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