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Rat Hemopexin. Molecular cloning, primary structural characterization, and analysis of gene expression

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00217a036· OSTI ID:5597097
;  [1];  [2]
  1. Cornell Univ., New York, NY (USA)
  2. Washington Univ., St. Louis, MO (USA)
A full-length hemopexin cDNA was isolated from a rat liver cDNA library and the derived amino acid sequence was obtained. Rat hemopexin shows a 76% amino acid homology with human hemopexin. The amino-terminal domain of rat hemopexin contains two histidine residues that are conserved in the human and rat sequences and are the most likely heme axial ligands. Analogous to human hemopexin, the rat hemopexin consists of 10 internal repeating peptide motifs characteristic of the pexin gene family. A complete conservation of cysteine residues is seen between the human and rat sequences suggesting an identical disulfide bridge structure in both proteins. The analysis of the primary structure of rat hemopexin reveals characteristics typical for members of the pexin gene family and suggest a conserved evolutionary role for the C-terminal (non-heme-binding) domain of this protein. The full-length rat hemopexin cDNA was used to analyze changes in hemopexin gene expression during development and experimental inflammation. RNA blot analysis showed a single 2.0-kb hemopexin mRNA present in fetal liver at day 14. The data also indicate that typical of the acute-phase response in rodents the regulation of hemopexin synthesis occurs at a pretranslational level. In contrast to many plasma proteins, hemopexin gene expression is entirely confined to the liver during development, inflammation, and tissue injury.
OSTI ID:
5597097
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:3; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English