Isolation and characterization of bovine haptoglobin from acute phase sera.

نویسندگان

  • M Morimatsu
  • B Syuto
  • N Shimada
  • T Fujinaga
  • S Yamamoto
  • M Saito
  • M Naiki
چکیده

A macromolecular hemoglobin-binding protein, which was not detectable in normal bovine sera but appeared during acute phase inflammation, was purified, characterized, and designated as bovine haptoglobin (Hp). The purified protein had a molecular mass of 1,000-2,000 kDa, and was composed of two kinds of peptides, a 20-kDa peptide (alpha chain) and a 35-kDa glycopeptide (beta chain) linked by disulfide bonds. Amino acid composition and N-terminal sequence analyses revealed that both peptides were homologous to each counterpart of human Hp. Studies using some reducing reagents proved that highly polymerized Hp in serum was composed of 2-20 polymerized forms of alpha 2 beta 2 tetramer. Hp could bind one molecule of hemoglobin/alpha 2 beta 2 unit. Hp with smaller sizes obtained from native Hp by partial reduction with cysteine showed almost the same Hb-binding capacity.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 266 18  شماره 

صفحات  -

تاریخ انتشار 1991