Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Assunta Brio"'
Autor:
Vincenzo Zappia, Giovanna Cacciapuoti, Assunta Brio, Marina Porcelli, Sabrina Forte, Maria Angela Moretti
Publikováno v:
FEBS Journal. 272:1886-1899
We report herein the first molecular characterization of 5′-deoxy-5′-methylthio-adenosine phosphorylase II from Sulfolobus solfataricus (SsMTAPII). The isolated gene of SsMTAPII was overexpressed in Escherichia coli BL21. Purified recombinant SsM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a63ebcf4c58f747cb7224cb23ae093d
https://doi.org/10.1111/j.1742-4658.2005.04619.x
https://doi.org/10.1111/j.1742-4658.2005.04619.x
Autor:
Giovanna, Cacciapuoti, Sabrina, Forte, Maria Angela, Moretti, Assunta, Brio, Vincenzo, Zappia, Marina, Porcelli
Publikováno v:
The FEBS journal. 272(8)
We report herein the first molecular characterization of 5'-deoxy-5'-methylthio-adenosine phosphorylase II from Sulfolobus solfataricus (SsMTAPII). The isolated gene of SsMTAPII was overexpressed in Escherichia coli BL21. Purified recombinant SsMTAPI
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::12b1d63eebf05f9bb6e878529f0110dc
https://pubmed.ncbi.nlm.nih.gov/15819883
https://pubmed.ncbi.nlm.nih.gov/15819883
Autor:
Sabrina Forte, Maria Angela Moretti, Vincenzo Zappia, Laura Camardella, Marina Porcelli, Assunta Brio, Giovanna Cacciapuoti
The extremely heat-stable 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus was cloned, expressed to high levels in Escherichia coli, and purified to homogeneity by heat precipitation and affinity chromatogr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10fea57d249d846b5bd075fffae7b43c
http://hdl.handle.net/11591/228793
http://hdl.handle.net/11591/228793
5′-Methylthioadenosine phosphorylase (MTAP) was purified to homogeneity from the hyperthermophilic archaeon Pyrococcus furiosus. The protein is a homoexamer of 180 kDa. The enzyme is highly thermoactive, with an optimum temperature of 125 °C, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc0d48acce77562272254cf44589e2e3
http://hdl.handle.net/11591/196838
http://hdl.handle.net/11591/196838