Detection of conformational changes in rat kidney gamma-glutamyl transpeptidase by an antibody against a synthetic peptide belonging to part of the reactive centre of the enzyme

G. A. Glass; E. Bluvshtein; Y. Gur; S. Sfez; V. Simovich; A. A. Stark

Detection of conformational changes in rat kidney gamma-glutamyl transpeptidase by an antibody against a synthetic peptide belonging to part of the reactive centre of the enzyme

G. A. Glass, E. Bluvshtein, Y. Gur, S. Sfez, V. Simovich, A. A. Stark^*

^*Corresponding author for this work

Biochemistry Molecular Biology

Tel Aviv University

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

3 Scopus citations

Abstract

Polyclonal antibodies were produced against rat kidney gamma-glutamyl transpeptidase (GGT) and against a synthetic peptide corresponding to residues 512-534 in rat GGT. The anti-peptide antibody bound denatured GGT, acivicin-treated GGT and GGT adsorbed to microtiter plates, but not GGT in solution, and did not inhibit GGT. The antibody against native GGT inhibited its activity in solution and did not bind efficiently adsorbed GGT in direct ELISA. It was active in direct and competition ELISA using kidney brush border membranes as the adsorbed antigen. The results indicate that these antibodies recognize conformational rather than sequence epitopes in GGT, and that marked changes occur in the conformation of GGT upon its adsorption to plates or its reaction with acivicin.

Original language	English
Pages (from-to)	505-513
Number of pages	9
Journal	Biochemistry and Molecular Biology International
Volume	33
Issue number	3
State	Published - 1994

Cite this

@article{d0b989c164c74ee9b97cd57cfc3978d6,

title = "Detection of conformational changes in rat kidney gamma-glutamyl transpeptidase by an antibody against a synthetic peptide belonging to part of the reactive centre of the enzyme",

abstract = "Polyclonal antibodies were produced against rat kidney gamma-glutamyl transpeptidase (GGT) and against a synthetic peptide corresponding to residues 512-534 in rat GGT. The anti-peptide antibody bound denatured GGT, acivicin-treated GGT and GGT adsorbed to microtiter plates, but not GGT in solution, and did not inhibit GGT. The antibody against native GGT inhibited its activity in solution and did not bind efficiently adsorbed GGT in direct ELISA. It was active in direct and competition ELISA using kidney brush border membranes as the adsorbed antigen. The results indicate that these antibodies recognize conformational rather than sequence epitopes in GGT, and that marked changes occur in the conformation of GGT upon its adsorption to plates or its reaction with acivicin.",

author = "Glass, {G. A.} and E. Bluvshtein and Y. Gur and S. Sfez and V. Simovich and Stark, {A. A.}",

year = "1994",

language = "אנגלית",

volume = "33",

pages = "505--513",

journal = "Biochemistry and Molecular Biology International",

issn = "1039-9712",

publisher = "John Wiley and Sons Inc.",

number = "3",

}

Detection of conformational changes in rat kidney gamma-glutamyl transpeptidase by an antibody against a synthetic peptide belonging to part of the reactive centre of the enzyme. / Glass, G. A.; Bluvshtein, E.; Gur, Y. et al.
In: Biochemistry and Molecular Biology International, Vol. 33, No. 3, 1994, p. 505-513.

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

TY - JOUR

T1 - Detection of conformational changes in rat kidney gamma-glutamyl transpeptidase by an antibody against a synthetic peptide belonging to part of the reactive centre of the enzyme

AU - Glass, G. A.

AU - Bluvshtein, E.

AU - Gur, Y.

AU - Sfez, S.

AU - Simovich, V.

AU - Stark, A. A.

PY - 1994

Y1 - 1994

N2 - Polyclonal antibodies were produced against rat kidney gamma-glutamyl transpeptidase (GGT) and against a synthetic peptide corresponding to residues 512-534 in rat GGT. The anti-peptide antibody bound denatured GGT, acivicin-treated GGT and GGT adsorbed to microtiter plates, but not GGT in solution, and did not inhibit GGT. The antibody against native GGT inhibited its activity in solution and did not bind efficiently adsorbed GGT in direct ELISA. It was active in direct and competition ELISA using kidney brush border membranes as the adsorbed antigen. The results indicate that these antibodies recognize conformational rather than sequence epitopes in GGT, and that marked changes occur in the conformation of GGT upon its adsorption to plates or its reaction with acivicin.

AB - Polyclonal antibodies were produced against rat kidney gamma-glutamyl transpeptidase (GGT) and against a synthetic peptide corresponding to residues 512-534 in rat GGT. The anti-peptide antibody bound denatured GGT, acivicin-treated GGT and GGT adsorbed to microtiter plates, but not GGT in solution, and did not inhibit GGT. The antibody against native GGT inhibited its activity in solution and did not bind efficiently adsorbed GGT in direct ELISA. It was active in direct and competition ELISA using kidney brush border membranes as the adsorbed antigen. The results indicate that these antibodies recognize conformational rather than sequence epitopes in GGT, and that marked changes occur in the conformation of GGT upon its adsorption to plates or its reaction with acivicin.

UR - http://www.scopus.com/inward/record.url?scp=0028199105&partnerID=8YFLogxK

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:0028199105

SN - 1039-9712

VL - 33

SP - 505

EP - 513

JO - Biochemistry and Molecular Biology International

JF - Biochemistry and Molecular Biology International

IS - 3

ER -

Detection of conformational changes in rat kidney gamma-glutamyl transpeptidase by an antibody against a synthetic peptide belonging to part of the reactive centre of the enzyme

Abstract

Other files and links

Fingerprint

Cite this