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Zoological Research
Kunming Institute of Zoology, Chinese Academy of Sciences
ISSN: 2095-8137
Vol. 29, No. 2, 2008, pp. 139-144
Bioline Code: zr08023
Full paper language: Chinese
Document type: Research Article
Document available free of charge

Zoological Research, Vol. 29, No. 2, 2008, pp. 139-144

 en Expression of Human Semenogelin I-52 and Antibacterial Activity Investigation of Recombinant Peptide
Zhao, Hui; Liu, Xiao-dong; Gao, Zhen-hua; Zhang, Jian-hua; Li, Hong; Zhang, Yun; Lee, Wen-hui & Shen, Ji-hong

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 DH5α after 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.

Keywords
Human; Semenogelin I; Expression; Antibacterial

 
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Alternative site location: http://www.zoores.ac.cn/

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