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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/43395

Title: Purification and characterization of cysteine proteinase inhibitors from crucian carp Carassius auratus eggs
Authors: Tzeng, S.S.;Wu, H.C.;Sung, W.C.;Liu, C.A
Contributors: 國立臺灣海洋大學:食品科學系
Date: 2009
Issue Date: 2017-07-27T02:57:35Z
Publisher: Fish Science
Abstract: 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 50degC, 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: 75, pp.1453-146
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/43395
Appears in Collections:[食品科學系] 期刊論文

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