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

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	1139-1146
Number of pages	8
Journal	Biochemistry and Molecular Biology International
Volume	32
Issue number	6
State	Published - 1994

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Genetics

Cite this

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

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.",

author = "A. Tonevitsky and A. Toptygin and I. Agapov and U. Pfueller and A. Frankel",

year = "1994",

language = "English (US)",

volume = "32",

pages = "1139--1146",

journal = "Biochemistry and Molecular Biology International",

issn = "1039-9712",

publisher = "Wiley-Blackwell",

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TY - JOUR

T1 - Renaturated ricin toxin B chain made in Escherichia coli is soluble, stable, and biologically active

AU - Tonevitsky, A.

AU - Toptygin, A.

AU - Agapov, I.

AU - Pfueller, U.

AU - Frankel, A.

PY - 1994

Y1 - 1994

N2 - 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.

AB - 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.

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M3 - Article

C2 - 8061631

AN - SCOPUS:0028356603

SN - 1039-9712

VL - 32

SP - 1139

EP - 1146

JO - Biochemistry and Molecular Biology International

JF - Biochemistry and Molecular Biology International

IS - 6

ER -

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

Abstract

ASJC Scopus subject areas

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