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Effects of phosphorylation on the kinetic properties of rat liver fructose-1,6-bisphosphatase.

A new purification procedure for rat liver fructose-1,6-bisphosphatase that involves use of Procion Red-Sepharose is described. The purified enzyme was homogeneous, had a subunit Mr of 40 000-41 000 and seemed to be undegraded. The enzyme could be phosphorylated by cyclic AMP-dependent protein kinas...

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Detalles Bibliográficos
Autores principales: Meek, D W, Nimmo, H G
Formato: Artigo
Lenguaje:Inglês
Publicado: 1984
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1144152/
https://ncbi.nlm.nih.gov/pubmed/6089751
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