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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
1999-2-3
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pubmed:abstractText |
IgG purified from sera of several patients with systemic lupus erythematosus and hepatitis B are shown to present RNA hydrolyzing activities that are different from the weak RNase A-type activities found in the sera of healthy donors. Further investigation brings evidence for two intrinsic activities, one observed in low salt conditions and another specifically stimulated by Mg2+ions and distinguishable from human sera RNases. Cleavage of RNA substrates by the latter activity is not sequence-specific but sensitive to both subtle conformational and/or drastic folding changes, as evidenced by comparative analysis of couples of structurally well-studied RNA substrates. These include yeast tRNAAsp and its in vitro transcript and human mitochondrial tRNALys-derived in vitro transcripts. The discovery of catalytic antibodies with RNase activities is a first step towards creation of a new generation of tools for the investigation of RNA structure.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Catalytic,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Asp,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Lys,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5243-50
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9826744-Antibodies, Catalytic,
pubmed-meshheading:9826744-Base Sequence,
pubmed-meshheading:9826744-Chromatography, Gel,
pubmed-meshheading:9826744-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9826744-Enzyme Activation,
pubmed-meshheading:9826744-Hepatitis B,
pubmed-meshheading:9826744-Hot Temperature,
pubmed-meshheading:9826744-Humans,
pubmed-meshheading:9826744-Hydrogen-Ion Concentration,
pubmed-meshheading:9826744-Hydrolysis,
pubmed-meshheading:9826744-Lupus Erythematosus, Systemic,
pubmed-meshheading:9826744-Magnesium,
pubmed-meshheading:9826744-Mitochondria,
pubmed-meshheading:9826744-Molecular Sequence Data,
pubmed-meshheading:9826744-Protein Denaturation,
pubmed-meshheading:9826744-RNA, Transfer, Asp,
pubmed-meshheading:9826744-RNA, Transfer, Lys,
pubmed-meshheading:9826744-Ribonucleases,
pubmed-meshheading:9826744-Saccharomyces cerevisiae,
pubmed-meshheading:9826744-Sodium,
pubmed-meshheading:9826744-Substrate Specificity,
pubmed-meshheading:9826744-Transcription, Genetic
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pubmed:year |
1998
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pubmed:articleTitle |
Characterization and selectivity of catalytic antibodies from human serum with RNase activity.
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pubmed:affiliation |
UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René Descartes, 67084 Strasbourg Cedex, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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