Výsledky vyhledávání - "J H, Ploemen"

Inhibition of glutathione conjugation by glutathione analogues in the perfused rat liver. Effect of esterification on the potency of gamma-L-glutamyl-alpha-(D-2-aminoadipyl)-N-2-heptylamine

Autor: S, Ouwerkerk-Mahadevan, R G, Tirona, R A, Ripping, J H, Ploemen, P J, van Bladeren, K S, Pang, J H, van Boom, G J, Mulder

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 25(10)

To assess the role of GST's (glutathione S-transferases) in the (de)toxification of their substrates, an in vivo active inhibitor based on the structure of glutathione (GSH), gamma-L-glutamyl-alpha-(D-2-aminoadipyl)-N-2-heptylamine monoethyl ester (E

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c67a7bf7d730589303d1fd525025e374
https://pubmed.ncbi.nlm.nih.gov/9321516

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Urinary thiodiacetic acid. A selective biomarker for the cytochrome P450-catalyzed oxidation of 1,2-dibromoethane in the rat

Autor: L W, Wormhoudt, J N, Commandeur, J H, Ploemen, R S, Abdoelgafoer, A, Makansi, P J, Van Bladeren, N P, Vermeulen

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 25(4)

1,2-Dibromoethane (1,2-DBE) is a carcinogenic compound that is metabolized both by cytochrome P450 (P450) and glutathione S-transferase (GST) enzymes, and that has been used by us as a model compound to study interindividual variability in biotransfo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::aaaa1e23f2446feaa34e690ff5c0dec5
https://pubmed.ncbi.nlm.nih.gov/9107551

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Identification of multiple target sites for a glutathione conjugate on glutathione-S-transferase by matrix-assisted laser desorption/ionization mass spectrometry

Autor: S, Jespersen, J H, Ploemen, P J, van Bladeren, W M, Niessen, U R, Tjaden, J, van der Greef

Publikováno v: Journal of mass spectrometry : JMS. 31(1)

A mass spectrometric method providing qualitative site-specific information regarding covalent modification of proteins is described. The method involves comparison of unmodified and modified proteins by matrix-assisted laser desorption/ionization ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a18e843b315f1d09d63f011bbf25c0d6
https://pubmed.ncbi.nlm.nih.gov/8925505

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Active-site tyrosyl residues are targets in the irreversible inhibition of a class Mu glutathione transferase by 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone

Autor: J H, Ploemen, W W, Johnson, S, Jespersen, D, Vanderwall, B, van Ommen, J, van der Greef, P J, van Bladeren, R N, Armstrong

Publikováno v: The Journal of biological chemistry. 269(43)

The mode of inactivation of glutathione S-transferase isoenzyme 3-3 from rat by the active site-directed inhibitor 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone (GSTCBQ) has been investigated by a combination of site-specific mutagenesis and ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::501e7fe0212a0426688ab2e9fe18952e
https://pubmed.ncbi.nlm.nih.gov/7929428

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Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1

Autor: J H, Ploemen, A, Van Schanke, B, Van Ommen, P J, Van Bladeren

Publikováno v: Cancer research. 54(4)

The reversibility of the conjugation reaction of the diuretic drug ethacrynic acid (EA), an alpha,beta-unsaturated ketone, with glutathione and glutathione S-transferase P1-1 (GST P1-1) has been studied. When the glutathione conjugate of EA was incub

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5e8ab096defca7627d5c192bb452fd62
https://pubmed.ncbi.nlm.nih.gov/8313381

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Active site-directed irreversible inhibition of glutathione S-transferases by the glutathione conjugate of tetrachloro-1,4-benzoquinone

Autor: B, van Ommen, C, den Besten, A L, Rutten, J H, Ploemen, R M, Vos, F, Müller, P J, van Bladeren

Publikováno v: The Journal of biological chemistry. 263(26)

Purified glutathione S-transferase from rat liver cytosol are irreversibly inhibited by the glutathione conjugate of tetrachloro-1,4-benzoquinone, 2-S-glutathionyl-3,5,6-trichloro-1,4-benzoquinone. The inhibition is due to covalent binding in or near

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::76d0bdf011390c9c175b49c2605c07d4
https://pubmed.ncbi.nlm.nih.gov/3417644

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