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An approach to optimizing the active site in a glutathione transferase by evolution in vitro.

A glutathione transferase (GST) mutant with four active-site substitutions (Phe(10)-->Pro/Ala(12)-->Trp/Leu(107)-->Phe/Leu(108)-->Arg) (C36) was isolated from a library of active-site mutants of human GST A1-1 by the combination of phage display and mechanism-based affinity adsorption [H...

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Hlavní autoři: Hansson, L O, Widersten, M, Mannervik, B
Médium: Artigo
Jazyk:Inglês
Vydáno: 1999
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1220618/
https://ncbi.nlm.nih.gov/pubmed/10548538
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