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赵晖, 刘孝东, 高振华, 张建华, 李 虹, 张云, 李文辉. 2008: 人精液凝固蛋白SgI-52的表达与抗菌活性研究. 动物学研究, 29(2): 139-144. DOI: 10.3724/SP.J.1141.2008.02139
引用本文: 赵晖, 刘孝东, 高振华, 张建华, 李 虹, 张云, 李文辉. 2008: 人精液凝固蛋白SgI-52的表达与抗菌活性研究. 动物学研究, 29(2): 139-144. DOI: 10.3724/SP.J.1141.2008.02139
ZHAO Hui, LIU Xiao-dong, GAO Zhen-hua, ZHANG Jian-hua, LI Hong, ZHANG Yun, LEE. 2008: Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide. Zoological Research, 29(2): 139-144. DOI: 10.3724/SP.J.1141.2008.02139
Citation: ZHAO Hui, LIU Xiao-dong, GAO Zhen-hua, ZHANG Jian-hua, LI Hong, ZHANG Yun, LEE. 2008: Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide. Zoological Research, 29(2): 139-144. DOI: 10.3724/SP.J.1141.2008.02139

人精液凝固蛋白SgI-52的表达与抗菌活性研究

Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide

  • 摘要: 以人精囊腺cDNA为模板, 用嵌套式PCR技术扩增出编码成熟人精液凝固蛋白I (semenogelin I, SgI)第85–136位氨基酸(SgI-52)的核苷酸序列并将其插入载体pMAL-p2X中, 成功构建的表达载体pMAL-p2X/SgI-52转化大肠杆菌DH5α后, 重组融合蛋白诱导表达于大肠杆菌周质中。经第X因子剪切及超滤处理,得到表达的重组SgI-52。质谱分析结果证明重组SgI-52为目的肽。重组人SgI-52对大肠杆菌ATCC 25922标准株以及耐氨苄标准株ML-35P的最低抑制浓度MIC分别为32.45以及46.30 μg/mL。我们的结果及相关研究提示在人精液液化过程中人精液凝固蛋白I的不同降解产物可能行使不同的生物学功能,值得进行深入研究。

     

    Abstract: Nucleotide sequence coding for SgI-52 with amino acid residues of 85-136 form mature human semenogelin I was amplified by PCR technique from the cDNA of a human seminal vesicle. The obtained PCR products were inserted into vector pMAL-p2X. The constructed expression vector of pMAL-p2X/SgI-52 was transformed into Escherichia coli DH5α. Fusion protein was expressed in the periplasma of the E. coli DH5αafter IPTG inducement. Recombinant SgI-52 was purified after factor X cleavage and a ultrafiltering process. MALDI-TOF- MS results indicated that the purified recombinant SgI-52 was the target peptide. Recombinant SgI-52 showed antibacterial activities on E. coli ATCC 25922 and E. coli ML-35P with MIC values of 32.45 and 46.30 μg/mL, respectively. Our results and other relevant works suggested that different human semenogelin I degradation fragments during the liquefaction might have various biological functions and deserve to be investigated further.

     

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