Expression and functional properties of genetically engineered ricin B chain lacking galactose-binding activity.

doi:10.1016/0167-4781(90)90035-z

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Article

Expression and functional properties of genetically engineered ricin B chain lacking galactose-binding activity.

Biochimica et biophysica acta - 21 Jun 1990

Vitetta E S, Yen N

Abstract excerpt

Ricin is a potent plant toxin consisting of two disulfide-bonded subunits. The A chain of ricin is an N-glycosidase which inactivates 28 S RNA and inhibits protein synthesis. The B chain is a galactose-specific lectin with two galactose-binding sites. The genes encoding preproricin and its A and B chains have been cloned and expressed. In addition, X-ray crystallographic studies have identified the...

Topics

Asialoglycoproteins
Base Sequence
Calcium-Binding Proteins
Carrier Proteins
DNA Mutational Analysis
Fetuins
Gene Expression
Glycoproteins
Molecular Sequence Data
Monosaccharide Transport Proteins
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligonucleotides

Periplasmic Binding Proteins

Radioimmunoassay

Recombinant Proteins

Ricin

Structure-Activity Relationship

Transfection

Source

Open in PubMed

Identifiers

PMID: 1694694
DOI: 10.1016/0167-4781(90)90035-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1694694-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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