Mutations of two lysine residues in the CDR loops of a recombinant immunotoxin that reduce its sensitivity to chemical derivatization.

doi:10.1021/bc00028a007

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Article

Mutations of two lysine residues in the CDR loops of a recombinant immunotoxin that reduce its sensitivity to chemical derivatization.

Bioconjugate chemistry - 1 Jan 2000

Benhar I, Brinkmann U, Webber K O, Pastan I

Abstract excerpt

B3(Fv)-PE38 is a recombinant single-chain immunotoxin in which the Fv region of monoclonal antibody B3 is connected to a truncated form of Pseudomonas exotoxin. It would be desirable to use the lysine residues of the molecule for chemical modification so that it can be derivatized with poly(ethylene glycol) to achieve reduced immunogenicity or with the Bolton-Hunter reagent for biodistribution studies. We found...

Topics

Amino Acid Sequence
Animals
Antibody Specificity
Arginine
Cell Survival
Escherichia coli
Glutamine
Humans
Immunoglobulin Variable Region
Immunotoxins
Iodine Radioisotopes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Lysine

Mice

Molecular Sequence Data

Mutation

Plasmids

Pseudomonas

Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 7948099
DOI: 10.1021/bc00028a007

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7948099-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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