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Characterization of S-adenosylhomocysteine hydrolase from Cryptosporidium parvum
Ctrnáctá V, Stejskal F, Keithly JS, Hrdý I
Jazyk angličtina Země Velká Británie
NLK
ProQuest Central
od 1996-01-01 do 2012-12-31
Medline Complete (EBSCOhost)
od 2006-01-01 do 2014-12-15
Health & Medicine (ProQuest)
od 1996-01-01 do 2012-12-31
Wiley Online Library (archiv)
od 1997-01-01 do 2012-12-31
Public Health Database (ProQuest)
od 1996-01-01 do 2012-12-31
Wiley Free Content
od 1997 do 2014
- MeSH
- adenin analogy a deriváty farmakologie MeSH
- adenosylhomocysteinasa antagonisté a inhibitory genetika chemie metabolismus MeSH
- Cryptosporidium parvum enzymologie genetika MeSH
- Escherichia coli genetika MeSH
- exprese genu MeSH
- financování organizované MeSH
- introny MeSH
- messenger RNA biosyntéza genetika MeSH
- molekulární sekvence - údaje MeSH
- molekulová hmotnost MeSH
- rekombinantní fúzní proteiny analýza genetika izolace a purifikace metabolismus MeSH
- RNA protozoální biosyntéza genetika MeSH
- sekvence aminokyselin MeSH
- sekvenční homologie aminokyselin MeSH
- vidarabin farmakologie MeSH
- vývojová regulace genové exprese MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
The S-adenosylhomocysteine hydrolase from the apicomplexan Cryptosporidium parvum (CpSAHH) has been characterized. CpSAHH is a single-copy, intronless gene of 1479 bp encoding a protein of 493 amino acids with a molecular mass of 55.6 kDa. Reverse transcriptase-polymerase chain reaction analysis confirmed that CpSAHH is expressed both in intracellular stages (in C. parvum-infected HCT-8 cells 24 h after infection) and in sporozoites. CpSAHH was expressed in Escherichia coli TB1 cells as a fusion with maltose-binding protein. The recombinant fusion was cleaved by Factor Xa and the enzymatic activity of both the fusion protein and the purified separated CpSAHH was measured. The enzymatic activity of CpSAHH was inhibited by d-eritadenine, S-DHPA and Ara-A.
Citace poskytuje Crossref.org
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- $a The S-adenosylhomocysteine hydrolase from the apicomplexan Cryptosporidium parvum (CpSAHH) has been characterized. CpSAHH is a single-copy, intronless gene of 1479 bp encoding a protein of 493 amino acids with a molecular mass of 55.6 kDa. Reverse transcriptase-polymerase chain reaction analysis confirmed that CpSAHH is expressed both in intracellular stages (in C. parvum-infected HCT-8 cells 24 h after infection) and in sporozoites. CpSAHH was expressed in Escherichia coli TB1 cells as a fusion with maltose-binding protein. The recombinant fusion was cleaved by Factor Xa and the enzymatic activity of both the fusion protein and the purified separated CpSAHH was measured. The enzymatic activity of CpSAHH was inhibited by d-eritadenine, S-DHPA and Ara-A.
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