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Purification and characterization of a heat-stable esterase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.

A heat-stable esterase has been purified 1080-fold to electrophoretic homogeneity from Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium; 20% of the starting activity is recovered. The purified enzyme shows a specific activity of 158 units/mg, based on the hydrolysis of p-nitrophenyl ac...

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Detalles Bibliográficos
Main Authors: Sobek, H, Görisch, H
Formato: Artigo
Idioma:Inglês
Publicado: 1988
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC1148878/
https://ncbi.nlm.nih.gov/pubmed/3128284
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