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The dipeptide, gamma-glutamylcysteine, is recognized by the anti-glutathione antibody single chain Fv fragment 20C9.

Abstract：

:The anti-glutathione antibody scFv 20C9, which we previously isolated from a human synthetic phage antibody scFv library [Hirose, M., Hayano, T., Shirai, H., Nakamura, H., and Kikuchi, M. (1998) Protein Eng. 11, 243-248], was expressed in the E. coli pET system and purified by sequential chromatography on Ni and glutathione-conjugated affinity resins. The purified scFv 20C9 antibody was characterized for its binding affinity for several glutathione derivatives by the BIACORE system. Although GSH, GSSG, and gamma-Glu-Cys could bind to the immobilized antibody, this was not the case for Cys-Gly, l-Glu, l-Cys, l-Gly, or several other glutathione derivatives such as gamma-Glu-Ser-Gly. The results suggest that a gamma-glutamic acid and sulfur atom are important for scFv 20C9 antibody recognition of glutathione. This is the first report to indicate that an scFv antibody can recognize a region as small as a dipeptide.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Horibe T,Furuya R,Iwai A,Yosho C,Tujimoto Y,Kikuchi M

doi

10.1006/bbrc.2001.4491

subject

Has Abstract

pub_date

2001-03-01 00:00:00

pages

1321-4

issue

5

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)94491-2

journal_volume

281

pub_type

杂志文章

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