Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/23244
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    Title: Purification and characterization of cysteine proteinase inhibitors from crucian carp Carassius auratus eggs
    Authors: Shinn-Shuenn Tzeng
    Hui-Chun Wu
    Wen-Chieh Sung
    Chien-An Liu
    Contributors: 餐旅管理系
    Keywords: Carassius auratus
    Crucian carp
    Cystatin
    Cysteine proteinase inhibitor
    Eggs
    Date: 2009-06
    Issue Date: 2010-11-17 17:07:10 (UTC+8)
    Abstract: 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.
    Relation: Fisheries Science 75(6):p.1453-1460
    Appears in Collections:[Dept. of Hotel and Restaurant Management] Periodical Articles

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