Document Detail


Recombinant cyclophilins lack nuclease activity.
MedLine Citation:
PMID:  15342605     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Several single-domain prokaryotic and eukaryotic cyclophilins have been identified as also being unspecific nucleases with a role in DNA degradation during the lytic processes that accompany bacterial cell death and eukaryotic apoptosis. Evidence is provided here that the supposed nuclease activity of human and bacterial recombinant cyclophilins is due to contamination of the proteins by the host Escherichia coli endonuclease and is not an intrinsic property of these proteins.
Authors:
Angel Manteca; Jesus Sanchez
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  186     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2004 Sep 
Date Detail:
Created Date:  2004-09-02     Completed Date:  2004-09-29     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6325-6     Citation Subset:  IM    
Affiliation:
Universidad de Oviedo, Departamento de Biología Funcional, Area de Microbiologia, Julian Claveria s/n, Oviedo 33006, Spain.
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MeSH Terms
Descriptor/Qualifier:
Cyclophilins / genetics*,  isolation & purification,  metabolism*
DNA / metabolism
Endodeoxyribonucleases / isolation & purification,  metabolism*
Escherichia coli / enzymology*,  metabolism*
Escherichia coli Proteins / isolation & purification,  metabolism
Recombinant Proteins / isolation & purification,  metabolism
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Recombinant Proteins; 9007-49-2/DNA; EC 3.1.-/Endodeoxyribonucleases; EC 5.2.1.-/Cyclophilins
Comments/Corrections

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