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Identification of an aminopeptidase from the skeletal muscle of grass carp (Ctenopharyngodon idellus)

文献类型： 外文期刊

作者： Zhou, Li-Gen 2 ; Liu, Bing-Xin 1 ; Sun, Le-Chang 1 ; Hara, Kenji 3 ; Su, Wen-Jin 1 ; Cao, Min-Jie 1 ;

作者机构： 1.Jimei Univ, Coll Biol Engn, Key Lab Sci & Technol Aquaculture & Food Safety, Xiamen 361021, Peoples R China

2.Zhejiang Acad Agr Sci, Inst Food Proc, Hangzhou 310021, Zhejiang, Peoples R China

3.Nagasaki Univ, Fac Fisheries, Nagasaki 8528521, Japan

关键词： Ctenopharyngodon idella;purification.;Aminopeptidase;Characterization;Internet resource.

期刊名称：FISH PHYSIOLOGY AND BIOCHEMISTRY （ 影响因子：2.794； 五年影响因子：2.876 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： Aminopeptidases play important roles in turnover of proteins, metabolism of hormones and neurotransmission, cell maturation and immunological regulations. In the present study, an aminopeptidase was purified to homogeneity from the skeletal muscle of grass carp by ammonium sulfate fractionation and sequential chromatographic steps, including DEAE-Sephacel, Sephacryl S-200, hydroxyapatite and Phenyl-Sepharose. The purified enzyme revealed a molecular mass of approximately 105 kDa both on SDS-PAGE and on gel filtration of Superdex 200. The enzymatic activity toward synthetic substrates was optimal at 40pC and pH 7.0-7.5. Metal-chelating agents such as EDTA and EGTA effectively inhibited the enzyme activity while inhibitors to serine, asparatic and cysteine proteinases did not show much effect, suggesting its belonging to metalloproteinase family. A specific aminopeptidase inhibitor bestatin was most effective in suppressing the enzymatic activity and performed in a competitive fashion. The enzymatic activity was slightly enhanced by metal ions of Mgpo and Mnpo while inhibited to different extents by Copo, Cupo, Znpo and Capo. Sulfhydryl reagent was necessary to maintain its activity. Purified enzyme demonstrated amidolytic activity most effectively against synthetic aminopeptidase substrate Leu-methylcoumarylamide (MCA) while N-terminal-blocked substrates and myofibrillar proteins were not hydrolyzed. The enzyme purified in the present study was quite possibly a leucine aminopeptidase (LAP) and functions during muscular protein metabolism.

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