宿半夏凝集素基因的克隆与分析  

Cloning and Analysis of Lectin Gene from Pinellia Ternata(Thunb.)Breit

作　　者：朱艳芳[1,2] 朱斌 梁志鹏 董庆 薛涛 盛玮[1,2] ZHU Yanfang;ZHU Bin;LIANG Zhipeng;DONG Qing;XUE Tao;SHEGN Wei(School of Life Science,Huaibei Normal University,235000,Huaibei,Anhui,China;Anhui Provincial Engineering Laboratory for Efficient Utilization of Featured Resource Plants,235000,Huaibei,Anhui,China)

机构地区：[1]淮北师范大学生命科学学院,安徽淮北235000 [2]安徽省特色资源植物利用工程实验室,安徽淮北235000

出　　处：《淮北师范大学学报（自然科学版）》2022年第4期70-76,共7页Journal of Huaibei Normal University：Natural Sciences

基　　金：国家自然科学基金项目(81803665);作物抗逆育种与减灾国家地方联合工程实验室开放课题(NELCOF20210102);国家级大学生创新创业项目(202110373022)。

摘　　要：半夏凝集素具有多种功能,为了深入研究和开发利用宿半夏凝集素(PTA),本研究克隆宿半夏凝集素基因(PtPTA).以宿半夏块茎为试验材料,通过PCR扩增得到PtPTA全长序列并分析. PtPTA开放阅读框为810bp,编码269个氨基酸,N-端有24个氨基酸残基的信号肽,总分子量为29 285.25,理论等电点为6.58,带负电氨基酸残基(Asp+Glu)总数为23,带正电氨基酸残基(Arg+Lys)总数为22,属于稳定的亲水蛋白.该蛋白与其他6种半夏凝集素氨基酸序列相似度达97.82%,具有典型的跨膜结构域,属于跨膜亲水蛋白,预测定位于细胞膜.本研究获得宿半夏凝集素基因的全长序列,为其功能的深入研究及开发利用奠定基础.Pinellia ternata lectin has many functions.In order to further study and develop Pinellia ternata lec⁃tin(PTA),the P.ternata lectin gene(PtPTA)was cloned in this study.The full-length sequence of PtPTA was amplified by PCR and analyzed.Open reading frame of PtPTA was 810 bp,encoding 269 amino acids.There was a signal peptide with 24 amino acid residues at the N-end of PTA.The total molecular weight was 29285.25,and the theoretical isoelectric point was 6.58.There were 23 negatively charged amino acid residues(ASP+Glu)and 22 positively charged amino acid residues(Arg+Lys)in PTA.So it was a stable hy⁃drophilic protein.The amino acid sequence similarity was 97.82%between PTA and the other six P.ternata lectins.PTA had a typical transmembrane domain and belonged to transmembrane hydrophilic protein,which was predicted to be located in the cell membrane.In this study,the full-length sequence of PtPTA was ob⁃tained,which laid a foundation for the in-depth study,development and utilization of PTA.

关 键 词：宿半夏 凝集素 基因克隆 生物信息学分析 

分 类 号：Q78[生物学—分子生物学]