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

Ji Young Kim, Hyun Jong Yang, Kwang Sig Kim, Young Bae Chung

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6 Scopus citations

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.

Original languageEnglish
Pages (from-to)157-160
Number of pages4
JournalThe Korean journal of parasitology
Volume43
Issue number4
DOIs
StatePublished - Dec 2005

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