Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes.
10.3347/kjp.2005.43.4.157
- Author:
Ji Young KIM
;
Hyun Jong YANG
;
Kwang Sig KIM
;
Young Bae CHUNG
- Publication Type:Brief Communication
- Keywords:
Taenia solium;
metacestode;
cysteine protease;
human IgG
- MeSH:
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
- From:The Korean Journal of Parasitology
2005;43(4):157-160
- CountryRepublic of Korea
- Language:English
-
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.
