乙二胺四乙酸
色谱法
化学
葡聚糖
酶
基质(水族馆)
十二烷基硫酸钠
酶动力学
酶分析
羧肽酶
聚丙烯酰胺凝胶电泳
大小排阻色谱法
钠
凝胶电泳
生物化学
生物
活动站点
螯合作用
生态学
有机化学
作者
Naourez Ktari,Hayet Ben Khaled,Imen Lassoued,Sofiane Ghorbel,Monçef Nasri
标识
DOI:10.1080/10498850.2012.708388
摘要
AbstractCarboxypeptidase B (CPB) from zebra blenny (Salaria basilisca) viscera was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration, with a 28-fold increase in specific activity and 21.72% recovery. The molecular weight of the enzyme was estimated to be 34.5 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH and temperature for the enzyme activity were around pH 8.0 and 60°C, respectively, using Hippuryl-l-Arg as a substrate. The enzyme was unstable above 50°C and below pH 5.0. The enzyme was activated by Co2+ and Zn2+ and inhibited by ethylenediaminetetraacetic acid (EDTA). The N-terminal amino acid sequence of the enzyme was determined as S P S Y T K Y N T. The CPB kinetic constants, Km and kcat for Hippuryl-l-Arg, were 0.32 mM and 36.23 s−1, respectively.Keywordszebra blenny (S. basilisca)carboxypeptidase Bpurificationcharacterization
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