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

FEBS Letters

Curstedt, Tore¹  Johansson, Jan²  Sjövall, Jan²  Gröndal, Staffan¹  Jörnvall, Hans² 

[1] Department of Clinical Chemistry, Karolinska Institutet at Danderyd Hospital, S-182 88 Danderyd, Sweden;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Serpin fragment;    Activation peptide;    Inactivation peptide;    Bile secretion;    Plasma peptide;   

DOI  :  10.1016/0014-5793(92)80234-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown