The complete amino acid sequence (703 amino acid residues) of human lactotransferrin has been determined. The location of the disulfide bridges has also been investigated. Computer analysis established internal homology of the two domains (residues 1-338 and residues 339-703). Each domain contains a single iron-binding site and a single glycosylation site (asparagine residues 137 and 490) located in homologous positions. Prediction of the secondary structure of the two homologous moieties of human lactotransferrin has also been performed. The present results allowed a series of comparisons to be made with human serum transferrin and hen ovotransferrin.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
The complete amino acid sequence (703 amino acid residues) of human lactotransferrin has been determined. The location of the disulfide bridges has also been investigated. Computer analysis established internal homology of the two domains (residues 1-338 and residues 339-703). Each domain contains a single iron-binding site and a single glycosylation site (asparagine residues 137 and 490) located in homologous positions. Prediction of the secondary structure of the two homologous moieties of human lactotransferrin has also been performed. The present results allowed a series of comparisons to be made with human serum transferrin and hen ovotransferrin.
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| skos:exactMatch | |
| uniprot:name |
Eur. J. Biochem.
|
| uniprot:author |
Jolles J.,
Jolles P.,
Legrand D.,
Mazurier J.,
Metz-Boutigue M.-H.,
Montreuil J.,
Schoentgen F.,
Spik G.
|
| uniprot:date |
1984
|
| uniprot:pages |
659-676
|
| uniprot:title |
Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins.
|
| uniprot:volume |
145
|
| dc-term:identifier |
doi:10.1111/j.1432-1033.1984.tb08607.x
|