Purification and characterization of cysteine proteinase inhibitors from crucian carp Carassius auratus eggs

doi:10.1007/s12562-009-0170-5

CNU IR > Human Ecology > Dept. of Hotel and Restaurant Management > Periodical Articles > Item 310902800/23244

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

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

Files in This Item:

File	Description	Size	Format
index.html		0Kb	HTML	1087	View/Open

Loading...