• Title/Summary/Keyword: Novoden modesrus

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Purification and Characterization of a Collagenolytic Protease from the Filefish, Novoden modestrus

  • Kim, Se-Kwon;Park, Pyo-Jam;Kim, Jong-Bae;Shahidi, Fereidoon
    • BMB Reports
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    • v.35 no.2
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    • pp.165-171
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    • 2002
  • A serine collagenolytic protease was purified from the internal organs of filefish Novoden modestrus, by ammonium sulfate, ion-exchange chromatography on a DEAE-Sephadex A-50, ion-exchange rechromatography on a DEAE-Sephadex A-50, and gel filtration on a Sephadex G-150 column. The molecular mass of the filefish serine collagenase was estimated to be 27.0 kDa by gel filtration and SDS-PAGE. The purified collagenase was optimally active at pH 7.0-8.0 and $55^{\circ}C$. The purified enzyme was rich in Ala, Ser, Leu, and Ile, but poor in Trp, Pro, Tyr, and Met. In addition, the purified collagenolytic enzyme was strongly inhibited by N-P-toluenesulfonyl-L-lysine chloromethyl ketone (TLCK), diisopropylfluorophosphate (DFP), and soybean trypsin inhibitor.