Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes.
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.
Kim
Ji Young
JY
Department of Parasitology, College of Medicine, Cheju National University, Jeju, Korea.
Yang
Hyun Jong
HJ
Kim
Kwang Sig
KS
Chung
Young Bae
YB
D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D019807:Iodoacetic Acid / Q000494:pharmacology; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D012710:Serum Albumin, Bovine / Q000378:metabolism; D041201:Taenia solium / Q000201:enzymology*
D015853:Cysteine Proteinase Inhibitors; D007074:Immunoglobulin G; D012710:Serum Albumin, Bovine; D003094:Collagen; D003546:Cysteine Endopeptidases; D007930:Leucine; C024974:E 64; D019807:Iodoacetic Acid