Linked Life Data

8001685

Source:http://linkedlifedata.com/resource/pubmed/id/8001685

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-1-23
pubmed:abstractText
Two electrophoretically distinct forms of superoxide dismutase (SOD; EC 1.15.1.1) which show different inhibition patterns to hydrogen peroxide have been identified in Azotobacter vinelandii. The SOD inhibited by hydrogen peroxide was purified to homogeneity, and turned out to be an iron superoxide dismutase. The enzyme is present in only one molecular form with an isoelectric point of 4.1, and it is composed of two identical subunits with an apparent molecular weight of 21,000 Da. Spectroscopic analyses indicated that this enzyme contains ferric iron (1.4-1.6 mol/mol protein) in the typical high-spin form present in other prokaryotic Fe-SODs. N-Terminal sequence alignments (up to the 49th residue) showed that A. vinelandii Fe-SOD has high similarity with other prokaryotic Fe-SODs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
357
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Purification and characterization of an iron superoxide dismutase from the nitrogen-fixing Azotobacter vinelandii.
pubmed:affiliation
Dipartimento di Scienze Molecolari Agroalimentari, CISMI, University of Milano, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't