Determination of intermediates, products and cleavage site in the reaction between plasminogen activator inhibitor type‐2 and urokinases

FEBS Letters

Kruithof, E.K.O.¹  Kaudewitz, H.²  Kiso, U.²  Henschen, A.²  Bachmann, F.¹  Åstedt, B.³ 

[1] Hematology Division, Department of Medicine, University Hospital Center, CHUV, 1011 Lausanne, Switzerland;Max Planck Institute for Biochemistry, 8033 Martinsried, FRG;Research Laboratories, Department of Gynecology and Obstetrics, University Hospital, 22185 Lund, Sweden

关键词: Plasminogen activator inhibitor;    Plasminogen activator;    Serpin;    Urokinase;    HPLC;    Amino acid sequence;    PAI-1 (−2);    type-1 (−2) plasminogen activator inhibitor;    u-PA;    urokinase-type plasminogen activator;    HPLC;    high-performance liquid chromatography;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(88)80640-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Several specific inhibitors for plasminogen activators have been isolated from various organs and cell lines, those from human placenta and the human monocyte-like cell line U-937 being virtually identical. The reaction between this type of inhibitor, designated as type-2, and high-M _r and low-M _r urokinase-type plasminogen activators was followed by reversed-phase high-performance liquid chromatography and gel electrophoresis. The components, their stable complexes and their dissociation and cleavage products could be clearly identified in both systems. The amino acid sequence of the inhibitor at the cleavage site was determined to be -Met-Thr-Gly-Arg↓Thr-Gly-His-Gly-. A 35-residue carboxy-terminal fragment was found to be released.

【 授权许可】

Unknown