Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Maria Angela Moretti"'
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
Publikováno v:
Algological Studies/Archiv für Hydrobiologie, Supplement Volumes. 95:31-42
The Internal Transcribed Spacer I (ITS1) of the nuclear ribosomal DNA of several taxa of Chlorella and of related species of Auxenochlorella, Graesiella, Mychonastes, and Scenedesmus has been sequenced. ITS 1 length ranges from 155 (S. fuscus) to 290
Autor:
Marina Porcelli, Phillip S. Brereton, Florian D. Schubot, John Rose, Vincenzo Zappia, Wolfram Tempel, Francesca Sorrentino, Luigi Concilio, Francis E. Jenney, Michael W. W. Adams, Giovanna Cacciapuoti, Bi-Cheng Wang, Zhi-Jie Liu, Maria Angela Moretti
We report here the characterization of the first agmatine/cadaverine aminopropyl transferase (ACAPT), the enzyme responsible for polyamine biosynthesis from an archaeon. The gene PF0127 encoding ACAPT in the hyperthermophile Pyrococcus furiosus was c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01f7c09e37a5b6d0d8161eea8fbeb892
http://hdl.handle.net/11591/188590
http://hdl.handle.net/11591/188590
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
Autor:
Antonello Merlino, Giuseppe Graziano, Giovanna Cacciapuoti, Luigi Concilio, Sabrina Forte, Marina Porcelli, Maria Angela Moretti
S-Adenosylhomocysteine hydrolase (AdoHcyHD) is an ubiquitous enzyme that catalyzes the breakdown of S-adenosylhomocysteine, a power- ful inhibitor of most transmethylation reactions, to adenosine and L-homocysteine. AdoHcyHD from the hyperthermophili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e60f06628f128572c539a880cbf76b0f
http://hdl.handle.net/11591/214930
http://hdl.handle.net/11591/214930
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
In this paper we report the cloning and sequencing of two small plasmids, pTAUp and pTADw, from the Antarctic Gram-negative Psychrobacter sp strain TA144. The observation that pTAUp contains a putative Rep-coding gene (Psyrep) suggested that its dupl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fa97e2b251c3e10baf350c9da85284c
http://hdl.handle.net/11588/480514
http://hdl.handle.net/11588/480514