Purification and characterization of pig inter- α-inhibitor and its constitutive heavy chains

• Published in: Biochimica et biophysica acta 1997-03, Vol.1338 (1), p.21-30
• Main Authors: Carrette, Odile, Mizon, Charlotte, Sautière, Pierre, Sesboüé, Richard, Mizon, Jacques
• Format: Article
• Language: English
• Subjects: Alpha-Globulins - chemistry; Alpha-Globulins - isolation & purification; Amino Acid Sequence; Animals; Bikunin; Cattle; Chromatography, Affinity; Chromatography, Ion Exchange; Cross Reactions; Electrophoresis, Polyacrylamide Gel; Humans; Hydroxylamine; Hydroxylamines; Inter- α-inhibitor; Macromolecular Substances; Mice; Molecular Sequence Data; Porcine plasma; Sequence comparison; Sequence Homology, Amino Acid; Serine Proteinase Inhibitors - chemistry; Swine
• ISSN: 0167-4838; 0006-3002; 1879-2588
• DOI: 10.1016/S0167-4838(96)00184-7

With the view of investigating the metabolism of inter- α-inhibitor, a plasma serine-proteinase inhibitor, in an animal model of inflammatory syndrome, we isolated inter- α-inhibitor from pig plasma. A high yield was obtained (140 mg/liter) with a two-step procedure: anion-exchange chromatography followed by affinity chromatography on heparin-Sepharose. In contrast to bovine inter- α-inhibitor, pig inter- α-inhibitor was highly similar to human inter- α-inhibitor: its heavy chains are homologous to the human H1 and H2 heavy chains, as shown by chromatographic and electrophoretic properties, cross-immunoreactivity and N-terminal sequencing. Pig may therefore represent a good animal model to study inter- α-inhibitor metabolism and elucidate its physiological role.