Halophilic 20S Proteasomes of the Archaeon Haloferax volcanii: Purification, Characterization, and Gene Sequence Analysis

A 20S proteasome, composed of α(1) and β subunits arranged in a barrel-shaped structure of four stacked rings, was purified from a halophilic archaeon Haloferax volcanii. The predominant peptide-hydrolyzing activity of the 600-kDa α(1)β-proteasome on synthetic substrates was cleavage carboxyl to hyd...

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Библиографические подробности

Опубликовано в::	J Bacteriol
Главные авторы:	Wilson, Heather L., Aldrich, Henry C., Maupin-Furlow, Julie
Формат:	Artigo
Язык:	Inglês
Опубликовано:	American Society for Microbiology (ASM) 1999
Предметы:	Enzymes and Proteins
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC94104/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10482525/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.181.18.5814-5824.1999
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