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    Please use this identifier to cite or link to this item: http://ir.cnu.edu.tw/handle/310902800/23244

    標題: Purification and characterization of cysteine proteinase inhibitors from crucian carp Carassius auratus eggs
    作者: Shinn-Shuenn Tzeng
    Hui-Chun Wu
    Wen-Chieh Sung
    Chien-An Liu
    貢獻者: 餐旅管理系
    關鍵字: Carassius auratus
    Crucian carp
    Cysteine proteinase inhibitor
    日期: 2009-06
    上傳時間: 2010-11-17 17:07:10 (UTC+8)
    摘要: Two cystatins (cst-I and cst-II) were purified from crucian carp eggs by acidification and subsequent ion exchange and molecular sieve chromatography. The molecular masses of cst-I and cst-II analyzed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis were 11.9 and 14.4 kDa, respectively, under reducing conditions and 13.5 and 12.7 kDa, respectively, under non-reducing conditions. The cst-I and cst-II molecules were stable after 30 min of incubation at 60 and 50°C, respectively. There was no significant loss in the inhibitory activity of either cst in the pH range 4–11. These two cystatins were able to affect the proteolysis of papain, cathepsin L, and bromelain, but they were unable to inhibit cathepsin B and trypsin. The partial N-terminal amino acid sequences of both cst inhibitors were homologous and that of cst-I was recognized as NH2-AGIPGGLVDADINDADVQ. This latter fragment shared 88.9% identity to common carp cystatin and 44.4–55.6% to cystatins of other aquatic animals. Based on these results, we conclude that the two cst inhibitors are members of family II cystatin.
    關聯: Fisheries Science 75(6):p.1453-1460
    Appears in Collections:[餐旅管理系] 期刊論文

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