CHOB
- CHOB的基本解释
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[医][=cyclophosphamide,Adriamycin,Oncovin bleomycin]环磷酰胺, 阿霉素, 长春新碱, 博莱霉
- 更多网络例句与CHOB相关的网络例句 [注：此内容来源于网络，仅供参考]
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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。
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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。
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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。
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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。