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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 |
1990-8-8
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pubmed:abstractText |
The amino acid sequence of hemerythrin from Siphonosoma cumanense was determined. The sequence consists of 113 amino acid residues. High homology is conserved in the regions of amino acid residues coordinating two iron atoms as its active site. The invariant sequences observed from the proteins in the same family were considerably altered except for the residues in the active site.
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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 |
Jun
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pubmed:issn |
0931-9506
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
141-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2362933-Amino Acid Sequence,
pubmed-meshheading:2362933-Amino Acids,
pubmed-meshheading:2362933-Animals,
pubmed-meshheading:2362933-Binding Sites,
pubmed-meshheading:2362933-Chromatography, High Pressure Liquid,
pubmed-meshheading:2362933-Hemerythrin,
pubmed-meshheading:2362933-Invertebrates,
pubmed-meshheading:2362933-Metalloendopeptidases,
pubmed-meshheading:2362933-Metalloproteins,
pubmed-meshheading:2362933-Molecular Sequence Data,
pubmed-meshheading:2362933-Sequence Homology, Nucleic Acid
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pubmed:year |
1990
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|
pubmed:articleTitle |
The amino acid sequence of hemerythrin from Siphonosoma cumanense.
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pubmed:affiliation |
Research Institute for Biosciences, Science University of Tokyo, Noda, Japan.
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pubmed:publicationType |
Journal Article
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