학술논문
Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins.
Document Type
Article
Author
Source
Subject
*LACTOFERRIN
*TRANSFERRIN
*AMINO acid sequence
*GLYCOSYLATION
*PROTEIN analysis
*BINDING sites
*IRON in the body
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Language
ISSN
0014-2956
Abstract
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. [ABSTRACT FROM AUTHOR]