[16] Preparation of Antibody—Toxin Conjugates

A. J. Cumber, J. A. Forrester, B. M J Foxwell, W. C J Ross, P. E. Thorpe

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

This chapter discusses the two ways of constructing antibody-toxin conjugates with cell-type specificity. The first is to link the antibody by a disulfide bond to the isolated A chain moiety or alternatively to one of the single-chain plant peptides, such as gelonin from Gelonium multiflorum, whose damaging action on eukaryotic ribosomes is apparently identical to that of the A chains of abrin and ricin. The second is to link the intact toxin to the antibody and block the cell recognition site on the B chain to prevent the conjugate from binding to and killing cells nonspecifically. This chapter describes the methods for preparing these two types of conjugate and characterizing them physicochemically and biologically. The chapter presents the advantages and limitations of a chain conjugates to those of intact toxin conjugates as selective cytotoxic agents in vitro and as chemotherapeutic agents in animals.

Original languageEnglish (US)
Pages (from-to)207-225
Number of pages19
JournalMethods in Enzymology
Volume112
Issue numberC
DOIs
StatePublished - Jan 1 1985

Fingerprint

Immunotoxins
Abrin
Ricin
Suregada
Antibodies
Cytotoxins
Disulfides
Animals
Ribosomes
Peptides
Gelonium multiflorum GEL protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Cumber, A. J., Forrester, J. A., Foxwell, B. M. J., Ross, W. C. J., & Thorpe, P. E. (1985). [16] Preparation of Antibody—Toxin Conjugates. Methods in Enzymology, 112(C), 207-225. https://doi.org/10.1016/S0076-6879(85)12018-5

[16] Preparation of Antibody—Toxin Conjugates. / Cumber, A. J.; Forrester, J. A.; Foxwell, B. M J; Ross, W. C J; Thorpe, P. E.

In: Methods in Enzymology, Vol. 112, No. C, 01.01.1985, p. 207-225.

Research output: Contribution to journalArticle

Cumber, AJ, Forrester, JA, Foxwell, BMJ, Ross, WCJ & Thorpe, PE 1985, '[16] Preparation of Antibody—Toxin Conjugates', Methods in Enzymology, vol. 112, no. C, pp. 207-225. https://doi.org/10.1016/S0076-6879(85)12018-5
Cumber AJ, Forrester JA, Foxwell BMJ, Ross WCJ, Thorpe PE. [16] Preparation of Antibody—Toxin Conjugates. Methods in Enzymology. 1985 Jan 1;112(C):207-225. https://doi.org/10.1016/S0076-6879(85)12018-5
Cumber, A. J. ; Forrester, J. A. ; Foxwell, B. M J ; Ross, W. C J ; Thorpe, P. E. / [16] Preparation of Antibody—Toxin Conjugates. In: Methods in Enzymology. 1985 ; Vol. 112, No. C. pp. 207-225.
@article{68fdd55da76f438aa5f4226dce25956c,
title = "[16] Preparation of Antibody—Toxin Conjugates",
abstract = "This chapter discusses the two ways of constructing antibody-toxin conjugates with cell-type specificity. The first is to link the antibody by a disulfide bond to the isolated A chain moiety or alternatively to one of the single-chain plant peptides, such as gelonin from Gelonium multiflorum, whose damaging action on eukaryotic ribosomes is apparently identical to that of the A chains of abrin and ricin. The second is to link the intact toxin to the antibody and block the cell recognition site on the B chain to prevent the conjugate from binding to and killing cells nonspecifically. This chapter describes the methods for preparing these two types of conjugate and characterizing them physicochemically and biologically. The chapter presents the advantages and limitations of a chain conjugates to those of intact toxin conjugates as selective cytotoxic agents in vitro and as chemotherapeutic agents in animals.",
author = "Cumber, {A. J.} and Forrester, {J. A.} and Foxwell, {B. M J} and Ross, {W. C J} and Thorpe, {P. E.}",
year = "1985",
month = "1",
day = "1",
doi = "10.1016/S0076-6879(85)12018-5",
language = "English (US)",
volume = "112",
pages = "207--225",
journal = "Methods in Enzymology",
issn = "0076-6879",
publisher = "Academic Press Inc.",
number = "C",

}

TY - JOUR

T1 - [16] Preparation of Antibody—Toxin Conjugates

AU - Cumber, A. J.

AU - Forrester, J. A.

AU - Foxwell, B. M J

AU - Ross, W. C J

AU - Thorpe, P. E.

PY - 1985/1/1

Y1 - 1985/1/1

N2 - This chapter discusses the two ways of constructing antibody-toxin conjugates with cell-type specificity. The first is to link the antibody by a disulfide bond to the isolated A chain moiety or alternatively to one of the single-chain plant peptides, such as gelonin from Gelonium multiflorum, whose damaging action on eukaryotic ribosomes is apparently identical to that of the A chains of abrin and ricin. The second is to link the intact toxin to the antibody and block the cell recognition site on the B chain to prevent the conjugate from binding to and killing cells nonspecifically. This chapter describes the methods for preparing these two types of conjugate and characterizing them physicochemically and biologically. The chapter presents the advantages and limitations of a chain conjugates to those of intact toxin conjugates as selective cytotoxic agents in vitro and as chemotherapeutic agents in animals.

AB - This chapter discusses the two ways of constructing antibody-toxin conjugates with cell-type specificity. The first is to link the antibody by a disulfide bond to the isolated A chain moiety or alternatively to one of the single-chain plant peptides, such as gelonin from Gelonium multiflorum, whose damaging action on eukaryotic ribosomes is apparently identical to that of the A chains of abrin and ricin. The second is to link the intact toxin to the antibody and block the cell recognition site on the B chain to prevent the conjugate from binding to and killing cells nonspecifically. This chapter describes the methods for preparing these two types of conjugate and characterizing them physicochemically and biologically. The chapter presents the advantages and limitations of a chain conjugates to those of intact toxin conjugates as selective cytotoxic agents in vitro and as chemotherapeutic agents in animals.

UR - http://www.scopus.com/inward/record.url?scp=0021891359&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021891359&partnerID=8YFLogxK

U2 - 10.1016/S0076-6879(85)12018-5

DO - 10.1016/S0076-6879(85)12018-5

M3 - Article

C2 - 3900635

AN - SCOPUS:0021891359

VL - 112

SP - 207

EP - 225

JO - Methods in Enzymology

JF - Methods in Enzymology

SN - 0076-6879

IS - C

ER -