Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1991-7-19
|
pubmed:abstractText |
The 70-amino-acid-residue N-terminal sequence of the bacterioferritin (BFR) of Azotobacter vinelandii was determined and shown to be highly similar to the N-terminal sequences of the Escherichia coli and Nitrobacter winogradskyi bacterioferritins. Electrophoretic and immunological analyses further indicate that the bacterioferritins of E. coli, A. vinelandii and Pseudomonas aeruginosa are closely related. A novel, two-subunit assembly state that predominates over the 24-subunit form of BFR at low pH was demonstrated. The results indicate that the bacterioferritins form a family of proteins that are distinct from the ferritins of plants and animals.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
1078
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
111-6
|
pubmed:dateRevised |
2009-9-29
|
pubmed:meshHeading |
pubmed-meshheading:1904771-Amino Acid Sequence,
pubmed-meshheading:1904771-Azotobacter,
pubmed-meshheading:1904771-Bacterial Proteins,
pubmed-meshheading:1904771-Chemistry, Physical,
pubmed-meshheading:1904771-Cross Reactions,
pubmed-meshheading:1904771-Cytochrome b Group,
pubmed-meshheading:1904771-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1904771-Escherichia coli,
pubmed-meshheading:1904771-Ferritins,
pubmed-meshheading:1904771-Immunodiffusion,
pubmed-meshheading:1904771-Isoelectric Focusing,
pubmed-meshheading:1904771-Molecular Sequence Data,
pubmed-meshheading:1904771-Nitrobacter,
pubmed-meshheading:1904771-Physicochemical Phenomena,
pubmed-meshheading:1904771-Pseudomonas aeruginosa,
pubmed-meshheading:1904771-Species Specificity
|
pubmed:year |
1991
|
pubmed:articleTitle |
Physical, chemical and immunological properties of the bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vinelandii.
|
pubmed:affiliation |
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, U.K.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|