Abstract
Affinity labeling, using reactive analogs of natural ligands, provides a powerful approach to probe for the existence of cooperative interactions between subunits as well as to locate specific xenobiotic binding sites in glutathione 5-transferases (GST). Thus, 3β-(iodoacetoxy)-dehydroisoandrosterone (3β-IDA) and 17-(iodoacetoxy)estradiol-3-sulfate (17β-IES) function as affinity labels of the nonsubstrate steroid binding site of rat liver GST, isozyme 1-1. Modification of Cys17 or Cys111 on Subunit A prevents reaction of the same cysteine on Subunit B. Interactions between the subunits of both the 4-4 and 1-1 isozymes are also illustrated by photoaffinity labeling of the active sites of these homodimers by glutathionyl S[4-(succinimidyl)-benzophenone], an analog of the product of glutathione and xenobiotic substrate.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 159-162 |
| Number of pages | 4 |
| Journal | Chemico-Biological Interactions |
| Volume | 133 |
| Issue number | 1-3 |
| State | Published - Feb 28 2001 |
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Keywords
- Affinity labeling
- Glutathione S-transferase
- Subunit interaction
ASJC Scopus subject areas
- Toxicology
Cite this
Probing subunit interactions in glutathione S-transferases using affinity labeling. / Colman, Roberta F.; Barycki, Joseph J.; Vargo, Melissa A.; Wang, Jibo.
In: Chemico-Biological Interactions, Vol. 133, No. 1-3, 28.02.2001, p. 159-162.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Probing subunit interactions in glutathione S-transferases using affinity labeling
AU - Colman, Roberta F.
AU - Barycki, Joseph J.
AU - Vargo, Melissa A.
AU - Wang, Jibo
PY - 2001/2/28
Y1 - 2001/2/28
N2 - Affinity labeling, using reactive analogs of natural ligands, provides a powerful approach to probe for the existence of cooperative interactions between subunits as well as to locate specific xenobiotic binding sites in glutathione 5-transferases (GST). Thus, 3β-(iodoacetoxy)-dehydroisoandrosterone (3β-IDA) and 17-(iodoacetoxy)estradiol-3-sulfate (17β-IES) function as affinity labels of the nonsubstrate steroid binding site of rat liver GST, isozyme 1-1. Modification of Cys17 or Cys111 on Subunit A prevents reaction of the same cysteine on Subunit B. Interactions between the subunits of both the 4-4 and 1-1 isozymes are also illustrated by photoaffinity labeling of the active sites of these homodimers by glutathionyl S[4-(succinimidyl)-benzophenone], an analog of the product of glutathione and xenobiotic substrate.
AB - Affinity labeling, using reactive analogs of natural ligands, provides a powerful approach to probe for the existence of cooperative interactions between subunits as well as to locate specific xenobiotic binding sites in glutathione 5-transferases (GST). Thus, 3β-(iodoacetoxy)-dehydroisoandrosterone (3β-IDA) and 17-(iodoacetoxy)estradiol-3-sulfate (17β-IES) function as affinity labels of the nonsubstrate steroid binding site of rat liver GST, isozyme 1-1. Modification of Cys17 or Cys111 on Subunit A prevents reaction of the same cysteine on Subunit B. Interactions between the subunits of both the 4-4 and 1-1 isozymes are also illustrated by photoaffinity labeling of the active sites of these homodimers by glutathionyl S[4-(succinimidyl)-benzophenone], an analog of the product of glutathione and xenobiotic substrate.
KW - Affinity labeling
KW - Glutathione S-transferase
KW - Subunit interaction
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UR - http://www.scopus.com/inward/citedby.url?scp=0000336613&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0000336613
VL - 133
SP - 159
EP - 162
JO - Chemico-Biological Interactions
JF - Chemico-Biological Interactions
SN - 0009-2797
IS - 1-3
ER -