Partial characterization of a cysteine protease from Panonychus citri |
Kyu-Hee Her1, Kwang-Sig KIM1, Gukmyung Choi2, Seung Hyoung Kim2, Young-Bae Chung3 |
1Departments of Surgery, Cheju National University College of Medicine, Jeju 690-756, Jeju, Korea 2Departments of Diagnostic Radiology, Cheju National University College of Medicine, Jeju 690-756, Jeju, Korea 3Departments of Parasitology, Cheju National University College of Medicine, Jeju 690-756, Jeju, Korea |
Correspondence:
Young-Bae Chung, Email: ybchung@cheju.ac.kr |
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Abstract |
A cysteine protease activity of Panonychus citri was detected and partially characterized. Proteolytic activity of the enzyme was enhanced by the addition of reducing agent, dithiothreitol (DTT), and also it was absolutely inhibited by cysteine protease specific inhibitors, such as trans-epoxy-succinyl-L-leucyl-amido (4-guanidino) butane (E.64) and iodoacetic acid (IAA). The other specific inhibitors of serine- and metallo-proteases could not inhibit the enzyme activity. This result showed for the first time cysteine protease activity of P. citri. Further studies on the biological roles of the enzyme are required. |
Key Words:
Panonychus citri , cysteine protease |
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