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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
1992-4-13
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pubmed:abstractText |
The iron-binding properties of melanotransferrin, the tumour-associated antigen also known as p97, have been investigated by UV/visible and fluorescence spectroscopy, amino acid sequence comparison, and modelling. These show that, in contrast to other transferrins, melanotransferrin binds only one Fe3+ ion per molecule. The binding properties of its N-terminal site are similar to other transferrins, but its C-terminal site does not bind iron at all. The differences can be related to specific amino acid changes in the C-terminal site.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
24
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pubmed:volume |
298
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
215-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1544447-Antigens, Neoplasm,
pubmed-meshheading:1544447-Binding Sites,
pubmed-meshheading:1544447-Humans,
pubmed-meshheading:1544447-Hydrogen-Ion Concentration,
pubmed-meshheading:1544447-Iron,
pubmed-meshheading:1544447-Melanoma,
pubmed-meshheading:1544447-Melanoma-Specific Antigens,
pubmed-meshheading:1544447-Neoplasm Proteins,
pubmed-meshheading:1544447-Protein Conformation,
pubmed-meshheading:1544447-Spectrometry, Fluorescence,
pubmed-meshheading:1544447-Tumor Cells, Cultured
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pubmed:year |
1992
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pubmed:articleTitle |
Human melanotransferrin (p97) has only one functional iron-binding site.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, Massey University, Palmerston North, New Zealand.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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