|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1993-6-29
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
A cDNA for pea glutathione reductase has been cloned and sequenced. The derived amino acid sequence of 562 residues shows a high degree of homology to the previously published GR sequences from human erythrocytes and from two prokaryotes: Escherichia coli and Pseudomonas aeruginosa. The pea enzyme differs from other GRs in having an N-terminal leader sequence of about 60-70 residues which may be a chloroplast transit peptide and a 20 amino acid C-terminal extension of unknown function.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0960-7412
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
2
|
|
pubmed:geneSymbol |
GR
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
129-31
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:1303792-Amino Acid Sequence,
pubmed-meshheading:1303792-Cloning, Molecular,
pubmed-meshheading:1303792-DNA,
pubmed-meshheading:1303792-Escherichia coli,
pubmed-meshheading:1303792-Fabaceae,
pubmed-meshheading:1303792-Glutathione Reductase,
pubmed-meshheading:1303792-Humans,
pubmed-meshheading:1303792-Molecular Sequence Data,
pubmed-meshheading:1303792-Plants,
pubmed-meshheading:1303792-Plants, Medicinal,
pubmed-meshheading:1303792-Pseudomonas aeruginosa,
pubmed-meshheading:1303792-Sequence Homology, Amino Acid,
pubmed-meshheading:1303792-Species Specificity
|
|
pubmed:year |
1992
|
|
pubmed:articleTitle |
Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).
|
|
pubmed:affiliation |
John Innes Institute, AFRC Institute of Plant Science Research, John Innes Centre, Norwich, UK.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|
