|本期目录/Table of Contents|

[1]段雪昆,杜翠红,胡健健,等.皱纹盘鲍Hdh-MMP-1基因cDNA的克隆及原核表达[J].集美大学学报(自然科学版),2016,21(5):321-329.
　DUAN Xue-kun,DU Cui-hong,HU Jian-jian,et al.cDNA Cloning and Prokaryotic Expression of Matrix Metalloproteinase-1 from Haliotis discus hannai[J].Journal of Jimei University,2016,21(5):321-329.
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《集美大学学报（自然科学版）》[ISSN:1007-7405/CN:35-1186/N]

卷:
第21卷
期数:
2016年第5期
页码:
321-329
栏目:
水产、食品与生物工程
出版日期:
2016-09-28

文章信息/Info

Title:
cDNA Cloning and Prokaryotic Expression of Matrix Metalloproteinase-1 from Haliotis discus hannai
作者:
段雪昆1; 杜翠红1; 2; 胡健健1; 蔡秋凤1; 2; 刘光明1; 2; 曹敏杰1; 2
(1.集美大学食品与生物工程学院，福建 厦门 361021;2.水产品深加工技术国家地方聚合工程研究中心，福建 厦门 361021)
Author(s):
DUAN Xue-kun1; DU Cui-hong1; 2; HU Jian-jian1; CAI Qiu-feng1; 2; LIU Guang-ming1; 2; CAO Min-jie1; 2
(1.College of Food and Biological Engineering，Jimei University，Xiamen 361021,China;2.National and Local Joint Engineering Research Center of Deep Processing Technology for Aquatic Products，Xiamen 361021,China)
关键词:
皱纹盘鲍; 基质金属蛋白酶; cDNA克隆; 生物信息学; 原核表达
Keywords:
Haliotis discus hannai; matrix metalloproteinases; cDNA cloning; bioinformatics;  prokaryotic expression
分类号:
-
DOI:
-
文献标志码:
A
摘要:
利用同源克隆方法和cDNA末端快速扩增(RACE)技术，从皱纹盘鲍(Haliotis discus hannai)肌肉组织中克隆得到基质金属蛋白酶-1基因(Hdh-MMP-1)cDNA全长序列(GenBank登录号：KR537291)。结果表明，Hdh-MMP-1 cDNA全长2136 bp，其中ORF长度为1551 bp，编码区含有516个氨基酸残基，预测其分子质量为58.94 ku，理论等电点为5.99。Hdh-MMP-1具有MMPs家族典型的N-端前肽区、催化区、铰链区和C-端类血红素结合区。利用SOPMA和SWISS-MODEL软件对该基因编码蛋白质高级结构进行了预测分析。氨基酸序列相似性结果显示，Hdh-MMP-1不仅与多种生物MMP-1基因具有序列相似性，且与某些软体动物和虫类的MMP-14及MMP-19也具有序列相似性。多序列比对结果显示，Hdh-MMP-1与红螺鲍、杂色鲍、美洲牡蛎的MMP-1相似性分别为95.29%、82.35%、38.85%。随后，构建了表达载体pET28a-catMMP-1，利用大肠杆菌原核表达系统，在大肠杆菌BL21 (DE3)中成功对该蛋白质催化区进行异源表达。
Abstract:
Matrix metalloproteinase-1 gene (Hdh-MMP-1)from the muscle of abalone(Haliotis discus hannai) was cloned by RT-PCR and RACE technology(GenBank accession number KR537291).The full-length of cDNA Hdh-MMP-1 was 2136 bp，including an open reading frame (ORF) of 1551 bp coding 516 amino acid residues with an estimated molecular weight of 58.94 ku and a theoretical pI of 5.99.The Hdh-MMP-1 contains N-terminal prodomain，catalytic domain，hinge region and C-terminal hemopexin domain，which was typical in matrix metalloproteinases.Higher-order structure of Hdh-MMP-1 was predicted using SOPMA and SWISS-MODEL.The results of multiple sequence alignment analysis showed that there was about 38.9%~95.3% identities in amino acid sequence with some other organisms.Prokaryotic expression plasmid pET28a-catMMP-1 containing the catalytic domain of MMP-1 was constructed.The recombinant MMP-1 was successfully expressed in Escherichia coli BL21cells.

参考文献/References:

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备注/Memo

备注/Memo:
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更新日期/Last Update: 2016-11-19