Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing

Ålin, Per; Jensson, Helgi; Guthenberg, Claes; Danielson, U. Helena; Tahir, Muhammad Aslam; Mannervik, Bengt

doi:10.1016/0003-2697(85)90545-7

Cited by 118 publications

(61 citation statements)

References 14 publications

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“…The increased activity with BSP may be ascribed specifically to an increased concentration of glutathione transferase subunit 3, since this is the only known subunit significantly active with this substrate [4,12,20]. The 2-fold elevated activity with t-PBO would similarly suggest an increased concentration of subunit 4 [4,12,20], but this interpretation is contradicted by a near 2-fold decrease in protein immunoprecipitable with antitransferase 4-4 antibodies (table 2). The remaining explanation appears to be that an as yet unidentified isoenzymes is responsible for the increased activity with t-PBO.…”

Section: Discussionmentioning

confidence: 99%

“…The remaining explanation appears to be that an as yet unidentified isoenzymes is responsible for the increased activity with t-PBO. The activities with CDNB and ethacrynic acid are less discriminatory among subunits, but it may be stated that none of the glutathione transferases of normal rat liver has a sufficiently high specific activity with ethacrynic acid [4,12,20] to explain the 5-fold increase in cytosolic activity (table 1). Evidently, the latter activity to a significant extent has to be ascribed to glutathione transferase 7-7 [l&19], demonstrated by its cross-reaction with antibodies to human transferase * (table 2).…”

Section: Discussionmentioning

confidence: 99%

“…After desalting on Sephadex G-25 packed in buffer A, the sample was concentrated by ultrafiltration to 14 ml. Four ml were used for chromatofocusing, performed as described by Alin et al [12].…”

Section: Isolation Of Basic Glutathione Transferasementioning

confidence: 99%

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Selective expression of glutathione transferase isoenzymes in chemically induced preneoplastic rat heptocyte nodules

1985

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Isoenzymes of glutathione transferase were shown to occur at selectively altered levels in rat hepatocyte nodules produced by 2-acetylaminofluorene treatment. Changes were measured by different substrates, antibodies raised against purified glutathione transferases, and by purification of the major isoenzymes. Isoenzymes composed of subunits 1,2 and 3, expressed in normal liver tissue, all occurred at increased concentrations in nodules, whereas the level of transferase 4-4 was decreased. The most conspicuous change was the appearance of glutathione transferase 7-7 (or transferase P), the concentration of which in negligible in normal liver. Glutathione transferase Hepatocyte nodule Isoenzyme induction Preneoplastic marker Immunoprecipitation

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Selective expression of glutathione transferase isoenzymes in chemically induced preneoplastic rat heptocyte nodules

1985

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“…The enzyme was purified from human placenta essentially as described elsewhere [13]. The enzymatic activity was measured at room temperature according to the method of Habig and Jakoby [141.…”

Section: Methodsmentioning

confidence: 99%

Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site‐directed fluorescent reagent

et al. 1990

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A fluorescent maleimide derivative, N-(4-anilino-l-naphthyl) maleimide (ANM), a specific probe for thiol groups, reacted with human placental glutathione transferase (GST, EC 2.5.1.18), causing a complete inactivation of the enzyme in a few minutes. The modified enzyme was denatured, alkylated and digested with (L-l-tosylamide-2-phenylethyl chloromethyl ketone)-trypsin. The tryptic digest was analysed by HPLC and a fluorescent peptide was obtained. The sequence of this peptide allowed us, by a comparison with a well known primary structure, to assign the position 47 to the most reactive cysteine of GST enzyme.

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“…Glutathione transferases from human placenta (19), human liver (20), rat liver (21), rat kidney (14), rat testis (13), and mouse liver (17) were purified to homogeneity by procedures as indicated. Antibodies to purified transferases were raised in rabbits.…”

mentioning

confidence: 99%

Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties.

Mannervik¹,

Ålin²,

Guthenberg³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

947

518

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The major isoenzymes of cytosolic glutathione transferase (EC 2.5.1.18) from rat, mouse, and man are shown to share structural and catalytic properties that can be used for species-independent classification. Rat, mouse, and human isoenzymes were grouped with respect to aminoterminal amino acid sequences, after correlation of seven structures analyzed in the present investigation with structures determined earlier. The isoenzymes were also characterized by substrate specificities and sensitivities to inhibitors, and the data were subjected to pattern recognition analysis. In addition, the various isoenzymes were tested for cross-reactivity by immunoprecipitation with antibodies raised against rat and human transferases. The different types of data were clearly correlated and afforded an unambiguous division of the isoenzymes into three classes named alpha, mu, and pi. Each of the three mammalian species studied contains at least one isoenzyme of each class. It is suggested that the similarities of the isoenzymes in a class reflect evolutionary relationships and that the classification applies generally.

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Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing

Cited by 118 publications

References 14 publications

Selective expression of glutathione transferase isoenzymes in chemically induced preneoplastic rat heptocyte nodules

Selective expression of glutathione transferase isoenzymes in chemically induced preneoplastic rat heptocyte nodules

Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site‐directed fluorescent reagent

Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties.

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