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Purification, Characterization, and Inhibitory Activity of Glassfish (Liparis tanakai) Egg High Molecular Weight Protease Inhibitor Against Papain and Cathepsin  

Ustadi Ustadi (Fisheries and Marine Department, Agriculture Faculty, Gadjah Mada University)
You Sang-Guan (Faculty of Marine Bioscience and Technology, Kangnung National University)
Kim Sang-Moo (Faculty of Marine Bioscience and Technology, Kangnung National University)
Publication Information
Journal of Microbiology and Biotechnology / v.16, no.4, 2006 , pp. 524-530 More about this Journal
Abstract
Two protease inhibitors of 67 and 18 kDa, respectively, were purified from the eggs of glass fish, Liparis tanakai, by affinity chromatography and electro-elution method. The high molecular weight (HMW) protein was purified with a specific inhibitory activity, yield, and purity of 18.46 U/mg, 0.07%, and 131.86 fold, respectively, and was further characterized: Optimal temperature and pH for inhibitory activity of the HMW glassfish egg protease inhibitor were $40^{\circ}C$ and pH 6, respectively, and it was stable between $5^{\circ}C\;and\;50^{\circ}C$ in the pH range of 5-6 with maximal stability at pH 6. It was shown to be a competitive inhibitor against papain with an inhibition constant $(K_i)$ of 97.02 nM. Moreover, the 67 kDa protein inhibited cathepsin, a cysteine protease, more effectively than did an egg-white protease inhibitor. The HMW glassfish egg protease inhibitor was classified as a member of the family III (kininogen).
Keywords
Glassfish egg; HMW protease inhibitor; $K_i$; kininogen;
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Times Cited By Web Of Science : 2  (Related Records In Web of Science)
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