Haptoglobin in Carnivora: a unique molecular structure in bear, cat and dog haptoglobins

Katsumi Mominoki, Noriko Nakagawa-Tosa, Masami Morimatsu, Bunei Syuto, Masayuki Saito

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


Haptoglobin (Hp), a hemoglobin-binding protein in plasma, consists of α and β subunits and has a tetra-chain arrangement (β-α-α-β) connected by disulfide bridges in most mammals so far examined. Dog Hp has been reported to be unique compared with other Hps in respect that (1) the two αβ units are joined by a non-covalent interaction rather than a disulfide bridge and (2) the α chain has an oligosaccharide-binding sequence (Asn-X-Ser/Thr) and is glycosylated. To determine whether the unique structures of dog Hp are common in the Carnivora, we purified Hps from sera of bear and cat, and analyzed their subunit structure and partial amino acid sequences. The analyses by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, under both reducing and non-reducing conditions, revealed that bear and cat Hps have similar subunit arrangements to dog Hp, suggesting the absence of a disulfide bridge between two α chains. This was confirmed by amino acid sequence analysis of the α chains: that is, Cys15 participating in the inter-α chain disulfide bridge was replaced by Val in bear or Leu in cat and dog. Thus, the unique subunit arrangement of Hp reported in dog may be common in the Carnivora. In contrast to dog Hp, however, α chains of bear and cat Hps were found not to have the typical oligosaccharide binding sequence on their α chains and were not glycosylated.

Original languageEnglish
Pages (from-to)785-789
Number of pages5
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Issue number4
Publication statusPublished - Apr 1995
Externally publishedYes


  • Bear
  • Carnivora
  • Cat
  • Disulfide bridge
  • Dog
  • Glycosylation
  • Haptoglobin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology


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