Renaturated ricin toxin B chain made in Escherichia coli is soluble, stable, and biologically active

A. Tonevitsky, A. Toptygin, I. Agapov, U. Pfueller, A. Frankel

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Escherichia coli cells transformed with plasmids containing ricin B-chain coding sequences are shown to express this heterologous protein in inclusion bodies. After denaturation and renaturation of the product in the presence of glutathione and lactose, the recombinant ricin B-chain is soluble, biologically active and stable. Cytotoxicity of heterodimer with this protein and ricin A-chain is bound to be only ten times less than of native ricin. Recombinant B-chain alone was nontoxic to cells (ID50 > 10-6M). Our data suggest that N-glycosylation of ricin B-chain is not required for its biological activity.

Original languageEnglish (US)
Pages (from-to)1139-1146
Number of pages8
JournalBiochemistry and Molecular Biology International
Volume32
Issue number6
StatePublished - 1994

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Ricin
Escherichia coli
Glycosylation
Denaturation
Inclusion Bodies
Lactose
Cytotoxicity
Bioactivity
Glutathione
Proteins
Plasmids

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

Cite this

Renaturated ricin toxin B chain made in Escherichia coli is soluble, stable, and biologically active. / Tonevitsky, A.; Toptygin, A.; Agapov, I.; Pfueller, U.; Frankel, A.

In: Biochemistry and Molecular Biology International, Vol. 32, No. 6, 1994, p. 1139-1146.

Research output: Contribution to journalArticle

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