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Intramolecular ionic interactions of lysine residues and a possible folding domain in fructose diphosphate aldolase.

1. Treatment with methyl acetimidate was used to probe the topography of the tetrameric fructose 1,6-diphosphate aldolase from ox liver. A single treatment with imido ester in the presence or absence of 20mM-fructose 1,6-diphosphate caused the number of amino groups in the enzyme to fall to approx....

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Autores principales: Lambert, J M, Perham, R N, Coggins, J R
Formato: Artigo
Lenguaje:Inglês
Publicado: 1977
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1164474/
https://ncbi.nlm.nih.gov/pubmed/851425
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