Expression of recombinant Lym-I single-chain Fv in Escherichia coli

Kyung Bin Song; Misun Won; Claude F. Meares

Expression of recombinant Lym-I single-chain Fv in Escherichia coli

Kyung Bin Song, Misun Won, Claude F. Meares

Chemistry

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Lym-I single-chain Fv (sFv) can be used for targeted radiodiagnosis and therapy of B-lymphocytic malignancies. Lym-I sFv was constructed and expressed as a glutathione S-transferase fusion protein, using a (G₄S)₃ linker connecting the C-terminus of the V(H) domain and the N-terminus of the V(L) domain of Lym-I. Six histidine residues and an E Tag epitope were introduced at the C-terminus of the sFv. Lym-I sFv was purified with glutathione-Sepharose 4B affinity chromatography followed by digestion with thrombin. Lym-I sFv of 28 kDa was confirmed by Western blotting with anti-(E Tag) monoclonal antibody. An antigen binding assay of Lym-I and a CD study indicated that it is functionally active.

Original language	English (US)
Pages (from-to)	163-167
Number of pages	5
Journal	Biotechnology and Applied Biochemistry
Volume	28
Issue number	2
State	Published - 1998

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Biochemistry
Biotechnology

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title = "Expression of recombinant Lym-I single-chain Fv in Escherichia coli",

abstract = "Lym-I single-chain Fv (sFv) can be used for targeted radiodiagnosis and therapy of B-lymphocytic malignancies. Lym-I sFv was constructed and expressed as a glutathione S-transferase fusion protein, using a (G4S)3 linker connecting the C-terminus of the V(H) domain and the N-terminus of the V(L) domain of Lym-I. Six histidine residues and an E Tag epitope were introduced at the C-terminus of the sFv. Lym-I sFv was purified with glutathione-Sepharose 4B affinity chromatography followed by digestion with thrombin. Lym-I sFv of 28 kDa was confirmed by Western blotting with anti-(E Tag) monoclonal antibody. An antigen binding assay of Lym-I and a CD study indicated that it is functionally active.",

author = "Song, {Kyung Bin} and Misun Won and Meares, {Claude F.}",

year = "1998",

language = "English (US)",

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journal = "Biotechnology and Applied Biochemistry",

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T1 - Expression of recombinant Lym-I single-chain Fv in Escherichia coli

AU - Song, Kyung Bin

AU - Won, Misun

AU - Meares, Claude F.

PY - 1998

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N2 - Lym-I single-chain Fv (sFv) can be used for targeted radiodiagnosis and therapy of B-lymphocytic malignancies. Lym-I sFv was constructed and expressed as a glutathione S-transferase fusion protein, using a (G4S)3 linker connecting the C-terminus of the V(H) domain and the N-terminus of the V(L) domain of Lym-I. Six histidine residues and an E Tag epitope were introduced at the C-terminus of the sFv. Lym-I sFv was purified with glutathione-Sepharose 4B affinity chromatography followed by digestion with thrombin. Lym-I sFv of 28 kDa was confirmed by Western blotting with anti-(E Tag) monoclonal antibody. An antigen binding assay of Lym-I and a CD study indicated that it is functionally active.

AB - Lym-I single-chain Fv (sFv) can be used for targeted radiodiagnosis and therapy of B-lymphocytic malignancies. Lym-I sFv was constructed and expressed as a glutathione S-transferase fusion protein, using a (G4S)3 linker connecting the C-terminus of the V(H) domain and the N-terminus of the V(L) domain of Lym-I. Six histidine residues and an E Tag epitope were introduced at the C-terminus of the sFv. Lym-I sFv was purified with glutathione-Sepharose 4B affinity chromatography followed by digestion with thrombin. Lym-I sFv of 28 kDa was confirmed by Western blotting with anti-(E Tag) monoclonal antibody. An antigen binding assay of Lym-I and a CD study indicated that it is functionally active.

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