Purification of epidermal plasminogen activator inhibitor

FEBS Letters

Hibino, Toshihiko¹  Izaki, Seiichi¹  Izaki, Masakatsu¹ 

[1] Department of Dermatology, Iwate Medical University School of Medicine, 19-1 Uchimaru, Morioka, Iwate 020, Japan

关键词: Plasminogen activator Enzyme inhibitor Urokinase Tissue-type plasminogen activator Binding inhibition;   

DOI  :  10.1016/0014-5793(86)81031-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A plasminogen activator inhibitor was purified from human cornified cell extract by DEAE-Sepharose, Sephacryl S-200, and high-performance liquid chromatographies on hydroxyapatite HPHT and anion-exchanger Mono Q at pH 7.2 and 8.0. The purified inhibitor showed M _r 43000 and pI 5.2. 50% inhibition of fibrinolytic activity (1.5 IU) of urokinase and tissue-type plasminogen activator was attained by 0.60 ng and 11.0 ng purified inhibitor respectively. Synthetic substrate assay demonstrated slow tight-binding inhibition to both urokinase and tissue-type plasminogen activator. The inhibitor did not inactivate plasmin, thrombin, glandular kallikrein or trypsin.

【 授权许可】

Unknown