Properties of Calpain II from Tilapia Muscle : Tilapia nilotica×Tilapia aurea(Food & Nutrition)
スポンサーリンク
概要
- 論文の詳細を見る
The characteristics of calpain II (EC 3.4.22.17) were investigated in order to clarify the function of this enzyme in post-mortem fish muscle. Calpain II purified from tilapia muscle (Tilapia nihtica×Tilapia aurea) was activated by Ca, Sr, Ba, and Mn, but inhibited by Fe, Co., Ni, Cu, Zn, Cd and Hg ions. This proteinase was unaffected by Na, K and Mg ions. The calcium ion might induce conformational changes and consequently activate this proteinase. The optimal pH and temperature for the activity were 7.5 and 30℃, respectively. Water activity and the ionic strength of the reaction solution significantly affected the activity of calapin II. Increasing ethylene glycol and polyethylene glycol significantly decreased the activity of calpain II. However, no significant effect on calpain II activity was apparent from the addition of nucleotides and their related compounds.
- 社団法人日本農芸化学会の論文
- 1991-02-23
著者
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Jiang Shann-tzong
Graduate School Of Marine Food Science National Taiwan Ocean University
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Wang Jeng-Hwan
Graduate School of Marine Food Science, National Taiwan Ocean University
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Wang Jeng-hwan
Graduate School Of Marine Food Science National Taiwan Ocean University
関連論文
- Comparison of the Cathepsin D from Mackerel (Scomber australasicus) and Milkfish(Chanos chanos) Muscle^+
- Substrate and Calcium Effects on the Autolysis of Tilapia Muscle m-Calpain
- Properties of Calpain II from Tilapia Muscle : Tilapia nilotica×Tilapia aurea(Food & Nutrition)