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CHOB相关的网络例句
与 CHOB 相关的网络例句 [注:此内容来源于网络,仅供参考]

The optimum temperatures for hydrolysis of the chitosanases were determined to be 52 for ChoA and 48 for ChoB, respectively.

两种壳聚糖酶最适反应pH值均为pH4.0,在pH 3.0—5.0的酸性环境中保持稳定。

Two inducible and extracellular chitosanases secreted by Penicillium sp. D-l were purified by ammonium sulfate precipitation as well as gel filtration. The purified enzymes of ChoA and ChoB had molecular masses of 93 and 21 kDa by SDS-PAGE. Both ChoA and ChoB have an acidic pH optimum, which were 4.0. The enzymes were stable over the pH range 3 to 5 for 1 h.

采用(NH_4)_2SO_4盐析法和凝胶过滤层析对Penicillium sp.D-1的壳聚糖酶进行分离提纯,得到两种壳聚糖酶,酶A经变性聚丙烯酰胺凝胶电泳分析,结果显示该酶的分子量约为93 kD;酶B经非变性聚丙烯酰胺凝胶电泳和SDS-PAGE分析,得出分子量约为21 kD。

Metal ions of Mn2+ stimulate the ChoA activity and Ca2+ significantly stimulate the ChoB activity, while Cu2+, Fe3+, and Ag+ inhibited them.

酶A的活性能够被Mn~(2+)激活,酶B的活性则能够被Ca~(2+)激活,Cu~(2+),Fe~(3+)和Ag~+则对两种酶的活性都有抑制作用。

The Km and Vmax were 7.35 mg/ml and 0.206 nmol/min-mg for ChoA, and 30.42 mg/ml and 0.376xmol/min-mg for ChoB, respectively. A 270bp DNA fragment, the partial chitosanase gene from Penicillium sp.

酶A的米氏常数K_m及最大反应速度V_分别为7.35 mg/ml、0.206 μmol/min·mg,酶B的米氏常数K_m及最大反应速度V_分别是30.42 mg/ml、0.376μmol/min·mg。

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然而现在,所有的孩子都要在综合学校继续学习,所以这次考试只是决定他们将要学习哪些课程。

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Detailed Intrinsic Reaction Coordination calculations were carried out to guarantee the optimized transition-state structures being connected to the related tautomers.

同时,做了详尽的内禀反应坐标计算,以保证所得到的过渡态连接相应的始末异构体。