Φορτώνει......
Inhibition and recognition studies on the glutathione-binding site of equine liver glutathione S-transferase.
Equine liver glutathione S-transferase has been shown to consist of two identical subunits of apparent Mr 25,500 and a pl of 8.9. Kinetic data at pH 6.5 with 1-chloro-2,4-dinitrobenzene as a substrate suggests a random rapid-equilibrium mechanism, which is supported by inhibition studies using gluta...
Αποθηκεύτηκε σε:
| Κύριος συγγραφέας: | |
|---|---|
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
1990
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1149527/ https://ncbi.nlm.nih.gov/pubmed/2222409 |
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