Purification and characterization of two functional forms of intracellular protease PfpI from the hyperthermophilic archaeon Pyrococcus furiosus
Article Abstract:
Purification of two functional forms of intracellular protease P. furiosus protease I (PfpI) from the cell extracts of hyperthermophilic archaeon Pyrococcus furiosus reveals special characteristics. The predominant purified form is PfpI-C1, which is a hexamer and accounts for 90% of the total activity. The minor purified form, PfpI-C2, is a trimeric. The composition of both the forms is similar to that of PfpI purified by heat treatment. The proteolytic and half-life activities, thermal stability, substrates, and temperature optimum ranges of the two forms are discussed.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
User Contributions:
Comment about this article or add new information about this topic:
Purification and characterization of a proteosome from the hyperthermophilic archaeon Pyrococcus furiosus
Article Abstract:
A four-step purification procedure was utilized for the isolation and characterization of the 20S proteosome of the thermophilic archaeon, Pyrococcus furiosus. The 640-kDa proteosome has a narrow substrate specificity when assayed with synthetic peptide substrates and contains an alpha (25-kDa) and a beta (22-kDa) subunit. Furthermore, the alpha and beta subunits of the proteosome were similar to the corresponding subunits of proteosomes from Thermoplasma acidophilum.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
User Contributions:
Comment about this article or add new information about this topic:
Growth of hyperthermophilic archaeon Pyrococcus furiosus on chitin involves two family 18 chitinases
Article Abstract:
Research has been conducted on Pyrococcus furiosus which grows on chitin. The authors report that chitin is a growth substrate for P. furiosus, and that the biochemical features of chitinase family have been determined for their recombinant forms.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp
- Abstracts: Purification and characterization of alpha-L-arabinofuranosidase from Bacillus stearothermophilus T-6. Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
- Abstracts: Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp. Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1
- Abstracts: Isolation and characterization of o-xylene oxygenase genes from Rhodococcus opacus TKN14. Isolation and characterization of thermophilic bacilli degrading cinnamic, 4-coumaric, and ferulic acids
- Abstracts: Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae