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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1989-6-16
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pubmed:abstractText |
Human H-chain ferritins bearing sequence changes in the 3-fold channels have been expressed in E. coli to investigate the role of these channels in iron-storage processes. The proteins assemble into shells resembling those of native ferritins. Iron uptake measurements indicate that residues in the 3-fold channels are involved neither in initial Fe(II)-oxidation nor in iron-core nucleation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
247
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
268-72
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:2714436-Amino Acid Sequence,
pubmed-meshheading:2714436-Crystallization,
pubmed-meshheading:2714436-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2714436-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:2714436-Ferritins,
pubmed-meshheading:2714436-Humans,
pubmed-meshheading:2714436-Iron,
pubmed-meshheading:2714436-Mutation,
pubmed-meshheading:2714436-Protein Conformation,
pubmed-meshheading:2714436-Recombinant Proteins,
pubmed-meshheading:2714436-Spectrophotometry, Ultraviolet,
pubmed-meshheading:2714436-Structure-Activity Relationship
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pubmed:year |
1989
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pubmed:articleTitle |
Recombinant H-chain ferritins: effects of changes in the 3-fold channels.
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pubmed:affiliation |
Department of Molecular Biology and Biotechnology, The University, Sheffield, England.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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