Source:http://linkedlifedata.com/resource/pubmed/id/12821328
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2003-6-24
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pubmed:abstractText |
The processing of human mitochondrial leucyl-tRNA synthetase had been previously investigated in insect cell. In the present work, the gene encoding human mitochondrial leucyl-tRNA synthetase with the same N-terminus as that processed in the mitochondria of insect cell was cloned and expressed in Escherichia coli. The enzyme was purified by affinity chromatography on Ni-NTA column. About 6 mg of human mitochondrial leucyl-tRNA synthetase was obtained from 1 liter of culture. The specific activity of the purified enzyme is 127.7 units/mg, the highest activity of the reported results; this enzyme has the potential for characterizing the mitochondrial tRNA mutants associated with some human mitochondrion-related neuromuscular disorders. The kinetic constants for three substrates: leucine, ATP, and E. coli tRNA1Leu (CAG) in the leucylation reaction are also reported herein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1046-5928
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
112-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12821328-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12821328-Escherichia coli,
pubmed-meshheading:12821328-Genetic Engineering,
pubmed-meshheading:12821328-Humans,
pubmed-meshheading:12821328-Kinetics,
pubmed-meshheading:12821328-Leucine-tRNA Ligase,
pubmed-meshheading:12821328-Mitochondria,
pubmed-meshheading:12821328-Recombinant Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Human mitochondrial leucyl-tRNA synthetase with high activity produced from Escherichia coli.
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pubmed:affiliation |
State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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