Wheat glutathione S-transferase: Purification and properties

G. Williamson; M. C. Beverley

doi:10.1016/S0733-5210(88)80026-2

Wheat glutathione S-transferase: Purification and properties

G. Williamson, M. C. Beverley

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

11 Citations (Scopus)

Abstract

Glutathione S-transferase (EC 2.5.1 .18) is present in wheat flour (0·07 mg enzyme/g flour). It was purified by hydrophobic interaction chromatography on phenyl Sepharose CL-4B and affinity chromatography on S-hexylglutathione Sepharose 6B. The enzyme is a homodimer with subunit molecular weight of 27500 and an isoelectric point of 5·9. It conjugated glutathione (K_m = 0·37 mm) with 1-chloro2,4-dinitrobenzene with a specific activity of 30μmol/min/mg protein. Linoleic acid hydroperoxides were reduced, with a specific activity of 60 nmol/min/mg protein for the 9-hydroperoxy-trans- 10,cis-l2-octadecadienoic acid isomer. The possible contribution of glutathione S-transferase to the baking properties of wheat is discussed.

Original language	English
Pages (from-to)	155-163
Number of pages	9
Journal	Journal of Cereal Science
Volume	8
Issue number	2
DOIs	https://doi.org/10.1016/S0733-5210(88)80026-2
Publication status	Published - 1 Jan 1988
Externally published	Yes

Keywords

1-chloro-2,4-dinitrobenzene
13-hydroperoxy-cis-9,trans-1 1-octadecadienoic acid
13c,t-HPO
9-hydroperoxy-trans- 10,cis-12-octadecadienoic acid
9c,t-HPO
CDNB
GSH
GSSG
oxidised glutathione
polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate
reduced glutathione
SDS-PAGE

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10.1016/S0733-5210(88)80026-2

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title = "Wheat glutathione S-transferase: Purification and properties",

abstract = "Glutathione S-transferase (EC 2.5.1 .18) is present in wheat flour (0·07 mg enzyme/g flour). It was purified by hydrophobic interaction chromatography on phenyl Sepharose CL-4B and affinity chromatography on S-hexylglutathione Sepharose 6B. The enzyme is a homodimer with subunit molecular weight of 27500 and an isoelectric point of 5·9. It conjugated glutathione (Km = 0·37 mm) with 1-chloro2,4-dinitrobenzene with a specific activity of 30μmol/min/mg protein. Linoleic acid hydroperoxides were reduced, with a specific activity of 60 nmol/min/mg protein for the 9-hydroperoxy-trans- 10,cis-l2-octadecadienoic acid isomer. The possible contribution of glutathione S-transferase to the baking properties of wheat is discussed.",

keywords = "1-chloro-2,4-dinitrobenzene, 13-hydroperoxy-cis-9,trans-1 1-octadecadienoic acid, 13c,t-HPO, 9-hydroperoxy-trans- 10,cis-12-octadecadienoic acid, 9c,t-HPO, CDNB, GSH, GSSG, oxidised glutathione, polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate, reduced glutathione, SDS-PAGE",

author = "G. Williamson and Beverley, {M. C.}",

year = "1988",

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doi = "10.1016/S0733-5210(88)80026-2",

language = "English",

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TY - JOUR

T1 - Wheat glutathione S-transferase

T2 - Purification and properties

AU - Williamson, G.

AU - Beverley, M. C.

PY - 1988/1/1

Y1 - 1988/1/1

N2 - Glutathione S-transferase (EC 2.5.1 .18) is present in wheat flour (0·07 mg enzyme/g flour). It was purified by hydrophobic interaction chromatography on phenyl Sepharose CL-4B and affinity chromatography on S-hexylglutathione Sepharose 6B. The enzyme is a homodimer with subunit molecular weight of 27500 and an isoelectric point of 5·9. It conjugated glutathione (Km = 0·37 mm) with 1-chloro2,4-dinitrobenzene with a specific activity of 30μmol/min/mg protein. Linoleic acid hydroperoxides were reduced, with a specific activity of 60 nmol/min/mg protein for the 9-hydroperoxy-trans- 10,cis-l2-octadecadienoic acid isomer. The possible contribution of glutathione S-transferase to the baking properties of wheat is discussed.

AB - Glutathione S-transferase (EC 2.5.1 .18) is present in wheat flour (0·07 mg enzyme/g flour). It was purified by hydrophobic interaction chromatography on phenyl Sepharose CL-4B and affinity chromatography on S-hexylglutathione Sepharose 6B. The enzyme is a homodimer with subunit molecular weight of 27500 and an isoelectric point of 5·9. It conjugated glutathione (Km = 0·37 mm) with 1-chloro2,4-dinitrobenzene with a specific activity of 30μmol/min/mg protein. Linoleic acid hydroperoxides were reduced, with a specific activity of 60 nmol/min/mg protein for the 9-hydroperoxy-trans- 10,cis-l2-octadecadienoic acid isomer. The possible contribution of glutathione S-transferase to the baking properties of wheat is discussed.

KW - 1-chloro-2,4-dinitrobenzene

KW - 13-hydroperoxy-cis-9,trans-1 1-octadecadienoic acid

KW - 13c,t-HPO

KW - 9-hydroperoxy-trans- 10,cis-12-octadecadienoic acid

KW - 9c,t-HPO

KW - CDNB

KW - GSH

KW - GSSG

KW - oxidised glutathione

KW - polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate

KW - reduced glutathione

KW - SDS-PAGE

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U2 - 10.1016/S0733-5210(88)80026-2

DO - 10.1016/S0733-5210(88)80026-2

M3 - Article

AN - SCOPUS:85009625117

VL - 8

SP - 155

EP - 163

JO - Journal of Cereal Science

JF - Journal of Cereal Science

SN - 0733-5210

IS - 2

ER -

Wheat glutathione S-transferase: Purification and properties

Abstract

Keywords

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