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Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme.

We have replaced the glutamic acid-165 at the active site of chicken triosephosphate isomerase with an aspartic acid residue using site-directed mutagenesis. Expression of the mutant protein in a strain of Escherichia coli that lacks the bacterial isomerase results in a complementation phenotype tha...

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Detalhes bibliográficos
Main Authors: Straus, D, Raines, R, Kawashima, E, Knowles, J R, Gilbert, W
Formato: Artigo
Idioma:Inglês
Publicado em: 1985
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC397539/
https://ncbi.nlm.nih.gov/pubmed/3887397
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