Identification of hydrophobic fragments of α1‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

Publisher Website
Google Scholar
Abstract
Hydrophobic peptides were isolated from the phospholipid fraction of human bile, plasma and spleen by exclusion chromatography in organic solvents. From plasma, the activation peptide or Cl protease inhibitor was recovered, from spleen the activation peptide of α1-antitrypsin, and from bile, both these peptides, as well as a fragment generated by proteolytic cleavage of α1-antitrypsin six residues N-terminal of the Pl–Pl ' peptide bond. Cleavages in this region inactivate antiproteases but have previously not been reported to occur in vivo. These peptides in human bile may reflect physiological actions in regulation of antiproteolytic activity or bile secretion processes, and/or be of importance for the physicochemical state of cholesterol, phospholipids and bile acids in bile.