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

김광식|정영배|김지영|양현종
대한기생충학ㆍ열대의학회 (The Korean Society For Parasitology and Tropical Medicine)|2005.12|Parasites, Hosts and Diseases|제43권 제4호|pp. 157-160

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참고문헌

주제분류예방의학/직업환경의학

초록

Abstract

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

참고문헌 (10)

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  3. "Activities of different cysteine proteases of Paragonimus westermani in cleaving human IgG", 35, pp.139~142 (1997)
  4. "Cysteine protease activities during maturation stages of Paragonimus westermani", 83, pp.902~907 (1997)
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관련 논문AI추천

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