Partial characterization of a 29kDa cysteine protease purified from Taenia solium metacestodes

  • KIM Ji-Young (Department of Parasitology, College of Medicine, Cheju National University) ;
  • YANG Hyun-Jong (Department of Parasitology, College of Medicine, Ewha Womans University) ;
  • KIM Kwang-Sig (Department of Surgery, College of Medicine, Cheju National University) ;
  • CHUNG Young-Bae (Department of Parasitology, College of Medicine, Cheju National University)
  • 발행 : 2005.12.01

초록

A 29kDa cysteine protease of Taenia solium metacestodes was purified by Mono Q anion-exchanger and Superose 6 HR gel filtration chromatography. The enzyme was effectively inhibited by cysteine protease inhibitors, such as iodoacetic acid (IAA) and trans-epoxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) while inhibitors acting on serine- or metallo-proteases did not affect the enzyme activity. The purified enzyme degraded human immunoglobulin G (IgG), collagen and bovine serum albumin (BSA), but human IgG was more susceptible for proteolysis by the enzyme. To define the precise biological roles of the enzyme, more detailed biochemical and functional studies would be required.

키워드

참고문헌

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