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http://dx.doi.org/10.5657/kfas.2005.38.2.083

Characteristics of Protease Inhibitor Purified from the Eggs of Alaska pollock (Theragra chalcogramma)  

STADI U (Department of Fisheries, Faculty of Agriculture, Gadjah Mada University)
KIM Keun Yeong (Faculty of Marine Bioscience & Technology, Kangnung National University)
KIM Sang Moo (Faculty of Marine Bioscience & Technology, Kangnung National University)
Publication Information
Korean Journal of Fisheries and Aquatic Sciences / v.38, no.2, 2005 , pp. 83-88 More about this Journal
Abstract
Protease inhibitors were purified from the eggs of Alaska pollock (Theragra chalcogramma) using the following purification steps: ammonium sulfate precipitation, ion exchange, gel permeation, and high performance liquid chromatographies (HPLC). The protease inhibitor from the heated eggs of Alaska pollock was not as well purified. In addition, the heated eggs showed lower specific inhibitory activity than the unheated eggs. The purification yields after ammonium sulfate precipitation, ion exchange, and gel permeation chromatographies were 22.7$\%,\;15.3\%$,and $4.4\%$, respectively. There were two kinds of protease inhibitors on the gel permeation chromatography pattern Their molecular weights were estimated to be 66,700 and 16,000 Da, respectively. Both were classified as a cysteine protease inhibitor because of the existence of inhibiting papain, which is one of cysteine proteases.
Keywords
Alaska pollock egg; cysteine protease; protease inhibitor; Theragra chalcogramma;
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