Korean J Parasitol.  2005 Dec;43(4):157-160. 10.3347/kjp.2005.43.4.157.

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

Affiliations
  • 1Department of Parasitology, College of Medicine, Cheju National University, Jeju 690-756, Korea. ybchung@cheju.ac.kr
  • 2Department of Parasitology, College of Medicine, Ewha Womans University, Seoul 158-710, Korea.
  • 3Department of Surgery, College of Medicine, Cheju National University, Jeju 690-756, Korea.

Abstract

A 29 kDa 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.

Keyword

Taenia solium; metacestode; cysteine protease; human IgG

MeSH Terms

Taenia solium/*enzymology
Serum Albumin, Bovine/metabolism
Leucine/analogs & derivatives/pharmacology
Iodoacetic Acid/pharmacology
Immunoglobulin G/metabolism
Humans
Cysteine Proteinase Inhibitors/pharmacology
Cysteine Endopeptidases/chemistry/*isolation & purification/metabolism
Collagen/metabolism
Chromatography, Ion Exchange
Chromatography, Gel
Animals
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