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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46549

Title: Purification and Characterization of Calpastatin from Grass Prawn Muscle (Penaeus monodon)
Authors: Shann-Tzong Jiang
Juwen Wu
Mei-Jui Su
Shinn-Shuenn Tzeng
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: grass prawn
calpain inhibitor
Calpastatin
Date: 2000
Issue Date: 2018-05-23T03:57:29Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract: Calpastatin, a specific calpain inhibitor was purified to electrophoretical homogeneity from grass prawn (Penaeus monodon) muscle by 100 °C heat-treatment, DEAE-Sephacel, and Q-Sepharose chromatographs. No significant change in the inhibitory activity of crude calpastatin was observed even after 20 min incubation at 100 °C, pH 7.0. The purified prawn calpastatin had a molecular weight (Mr) of 80 and 88.7 kDa determined by SDS−PAGE and Sephacryl S-200 HR gel filtration, respectively. According to the active site titration, the purified calpastatin revealed four beef μ-calpain and two beef m-calpain binding domains, respectively. It was stable during 1 h of incubation at 30 °C under pH 4.5−10.0 and shown to be a highly specific inhibitor for calpain.
Relation: 48(9) pp.3851–3856
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46549
Appears in Collections:[食品科學系] 期刊論文

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