Physicochemical Characterization of Synodontis schall Gills Rhodanese

E. Wodu, A. Frank-Oputu
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Abstract

The cyanide detoxifying enzyme, rhodanese was extracted from Synodontis schall gills and some physicochemical properties investigated. Activity of the enzyme preparation was assayed by measuring the activity of rhodanese in RU min-1 mg-1. The results revealed that Synodontis schall gills rhodanese had km values for KCN and Na2S2O3 as 22.73±4.12 and 16.67±5.31 respectively. The enzyme had higher affinity for Na2S2O3. Only ammonium sulphate displayed possible sulfur donating property but was less effective than thiosulphate. Synodontis schall gills rhodanese displayed maximum activity at pH 8.0 and 35֠ºC. Synodontis schall gills rhodanese was significantly (p<0.05) inhibited by PbCl2, BaCl2 and HgCl2 in a concentration dependent manner. Gills rhodanese of Synodontis schall was similar in properties to rhodanese extracted from other sources.
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罗丹岛小滑膜炎的理化性质
从鱼鳃中提取氰化物解毒酶罗丹斯,并对其理化性质进行了研究。通过测定RU min-1 mg-1中罗丹斯的活性来测定酶制剂的活性。结果表明,罗丹斯鱼对KCN和Na2S2O3的km值分别为22.73±4.12和16.67±5.31。该酶对Na2S2O3具有较高的亲和力。只有硫酸铵表现出可能的给硫性,但效果不如硫代硫酸铵。rhodanese小鳃滑膜炎在pH 8.0和35 ºC时表现出最大的活性。PbCl2、BaCl2和HgCl2对rhodanese小鳃滑膜炎(Synodontis schall gills rhodanese)有显著(p<0.05)抑制作用,且呈浓度依赖性。该鱼的罗丹斯鳃的性质与从其他来源提取的罗丹斯鳃相似。
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