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作 者:覃川杰[1,2] 陈立侨[1] 李二超[1] 杨洁萍[2] 姜雪芹[1]
机构地区:[1]华东师范大学生命科学学院,上海200062 [2]内江师范学院生物系,四川内江641000
出 处:《福建农林大学学报(自然科学版)》2013年第3期302-306,共5页Journal of Fujian Agriculture and Forestry University:Natural Science Edition
基 金:国家"973"计划资助项目(2009CB118702);国家科技支撑计划课题资助项目(2012BAD25B03);公益性行业(农业)科研专项资助项目(201203065);内江师范学院博士基金资助项目(09269)
摘 要:利用RT-PCR方法克隆瓦氏黄颡鱼(Pelteobagrus vachelli)肝脂酶cDNA序列片段,并对其基因结构和系统进化关系进行分析.瓦氏黄颡鱼肝脂酶cDNA片段长1065 bp,编码353个氨基酸.肝脂酶氨基酸序列同源性分析结果表明,瓦氏黄颡鱼与其他鱼类的同源性为62%-100%.瓦氏黄颡鱼肝脂酶氨基酸残基包含糖基化位点、催化位点、催化中心三联体位点、脂质结合位点和多肽"盖"等主要结构区域.系统进化树分析表明,瓦氏黄颡鱼肝脂酶与草鱼、鳙、斑马鱼肝脂酶聚为一支.因此,瓦氏黄颡鱼的肝脂酶在鱼类进化中较为保守.The partial cDNA sequence of hepatic lipase (HL) in darkbarbel catfish Pelteobagrus vacheUi was cloned by RT-PCR method. The obtained HL cDNA was 1065 hp and encoded 343 amino acids. Sequence comparison indicated that the deduced amino acid sequence of P. vachelli hepatic lipase had identity of 62% - 100% with that of other fish. The deduced amino acid sequence of P. vachetli hepatic hpase possessed conserved motif of the lipase gene superfamily, included the "lid" sites, potential N-linked glyeosylation sites, catalysis site, catalytic triad and putative lipid binding region. Phylogenetic analysis revealed that the P. vachelli hepatic lipase was closely related to the hepatic lipase in other fish.
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