Volume 29 Issue 2
Mar.  2008
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ZHAO Hui, LIU Xiao-dong, GAO Zhen-hua, ZHANG Jian-hua, LI Hong, ZHANG Yun, LEE. Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide. Zoological Research, 2008, 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. Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide. Zoological Research, 2008, 29(2): 139-144. doi: 10.3724/SP.J.1141.2008.02139

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

doi: 10.3724/SP.J.1141.2008.02139
  • Received Date: 2008-02-03
  • Rev Recd Date: 1900-01-01
  • Publish Date: 2008-04-22
  • 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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    沈阳化工大学材料科学与工程学院 沈阳 110142

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

doi: 10.3724/SP.J.1141.2008.02139

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.

ZHAO Hui, LIU Xiao-dong, GAO Zhen-hua, ZHANG Jian-hua, LI Hong, ZHANG Yun, LEE. Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide. Zoological Research, 2008, 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. Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide. Zoological Research, 2008, 29(2): 139-144. doi: 10.3724/SP.J.1141.2008.02139

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