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생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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Purification and Characterization of a Collagenolytic Protease from the Filefish, Novoden modestrus

  • Kim, Se-Kwon (Department of Chemistry, Pukyong National University) ;
  • Park, Pyo-Jam (Department of Chemistry, Pukyong National University) ;
  • Kim, Jong-Bae (Department of Sea-Food Science and Technology, Kunsan National University) ;
  • Shahidi, Fereidoon (Memorial University of Newfoundland)
  • 발행 : 2002.03.31
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초록

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.

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참고문헌

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