Isolation and purification of glutathione-S-transferase from the bulb mite Rhizoglyphus robini

Ephraim Cohen; Uri Gerson

doi:10.1016/0020-1790(86)90020-X

Isolation and purification of glutathione-S-transferase from the bulb mite Rhizoglyphus robini

Ephraim Cohen^*, Uri Gerson

^*Corresponding author for this work

Department of Plant Pathology and Microbiology

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

12 Scopus citations

Abstract

Glutathione-S-transferase from the cytosolic fraction of the bulb mite Rhizoglyphus robini has been purified to apparent homogeneity. The purification steps involved DEAE-Sepharose gel chromatography and glutathione-agarose affinity chromatography. The latter resulted in 94-fold purification and in 47% recovery of the enzyme activity present in the cytosol. The K_m values for l-chloro-2,4-dinitrobenzene and reduced glutathione were calculated to be 0.13 and 0.26 mM, respectively. Sodium dodecyl sulphate-polyacrylamide electrophoresis revealed one polypeptide band of 25,000 daltons molecular weight.

Original language	English
Pages (from-to)	449-454
Number of pages	6
Journal	Insect Biochemistry
Volume	16
Issue number	3
DOIs	https://doi.org/10.1016/0020-1790(86)90020-X
State	Published - 1986

Keywords

4-dinitrobenzene
Rhizoglyphus robini
glutathione
glutathione-S-transferase
glutathione-agarose affinity chromatography
l-Chloro-2

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10.1016/0020-1790(86)90020-X

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title = "Isolation and purification of glutathione-S-transferase from the bulb mite Rhizoglyphus robini",

abstract = "Glutathione-S-transferase from the cytosolic fraction of the bulb mite Rhizoglyphus robini has been purified to apparent homogeneity. The purification steps involved DEAE-Sepharose gel chromatography and glutathione-agarose affinity chromatography. The latter resulted in 94-fold purification and in 47% recovery of the enzyme activity present in the cytosol. The Km values for l-chloro-2,4-dinitrobenzene and reduced glutathione were calculated to be 0.13 and 0.26 mM, respectively. Sodium dodecyl sulphate-polyacrylamide electrophoresis revealed one polypeptide band of 25,000 daltons molecular weight.",

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T1 - Isolation and purification of glutathione-S-transferase from the bulb mite Rhizoglyphus robini

AU - Cohen, Ephraim

AU - Gerson, Uri

PY - 1986

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N2 - Glutathione-S-transferase from the cytosolic fraction of the bulb mite Rhizoglyphus robini has been purified to apparent homogeneity. The purification steps involved DEAE-Sepharose gel chromatography and glutathione-agarose affinity chromatography. The latter resulted in 94-fold purification and in 47% recovery of the enzyme activity present in the cytosol. The Km values for l-chloro-2,4-dinitrobenzene and reduced glutathione were calculated to be 0.13 and 0.26 mM, respectively. Sodium dodecyl sulphate-polyacrylamide electrophoresis revealed one polypeptide band of 25,000 daltons molecular weight.

AB - Glutathione-S-transferase from the cytosolic fraction of the bulb mite Rhizoglyphus robini has been purified to apparent homogeneity. The purification steps involved DEAE-Sepharose gel chromatography and glutathione-agarose affinity chromatography. The latter resulted in 94-fold purification and in 47% recovery of the enzyme activity present in the cytosol. The Km values for l-chloro-2,4-dinitrobenzene and reduced glutathione were calculated to be 0.13 and 0.26 mM, respectively. Sodium dodecyl sulphate-polyacrylamide electrophoresis revealed one polypeptide band of 25,000 daltons molecular weight.

KW - 4-dinitrobenzene

KW - Rhizoglyphus robini

KW - glutathione

KW - glutathione-S-transferase

KW - glutathione-agarose affinity chromatography

KW - l-Chloro-2

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JO - Insect Biochemistry

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ER -

Isolation and purification of glutathione-S-transferase from the bulb mite Rhizoglyphus robini

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