Linked Life Data

6386471

Source:http://linkedlifedata.com/resource/pubmed/id/6386471

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-12-20
pubmed:abstractText
The primary structure of calf thymus glutaredoxin was determined by analysis of the [14C]carboxymethylated protein and the proteolytic fragments obtained by treatments with trypsin, chymotrypsin, CNBr and staphylococcal Glu-specific extracellular protease. The active center has the structure Cys-Pro-Tyr-Cys, with the redox-active cysteines/half-cystines located at positions 22 and 25 in the polypeptide chain. This active center is identical in amino acid sequence and similar in position to that of Escherichia coli glutaredoxin, suggesting this structure to be typical for glutaredoxins and distinguishing them from the distantly related thioredoxins. However, the two glutaredoxins also exhibit considerable differences. Calf thymus glutaredoxin is extended at both ends and has 31% overall residue identities with the corresponding E. coli protein. In contrast to the bacterial glutaredoxin, the calf thymus protein contains two additional half-cystines/cysteine residues at positions 74 and 78, which may be of regulatory significance.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
417-23
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends and with an additional half-cystine/cysteine pair.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't