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Dive into the research topics where Su-Xia Li is active.

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Featured researches published by Su-Xia Li.


Molecular Biology Reports | 2011

A novel human derived cell-penetrating peptide in drug delivery.

Jian Zhao; Peng Gao; Wei Xiao; Li-Qiang Fan; Fu-Jun Wang; Su-Xia Li; Jian-Wen Liu

Cell-penetrating peptides can carry a variety of biologically active molecules into cells. Here we have identified a novel CPP derived from the C-terminus of human extracellular superoxide dismutase (hC-SOD3) which was shown to be located throughout in the cytoplasm and nucleus by fluorescence microscopy investigation. Furthermore, when apoptin fused to hC-SOD3, it was translocated efficiently into HeLa cells resulting in antitumor activities. This study shows that hC-SOD3 has the potential to penetrate and translocate cargo molecules into cells and has no cytotoxicity at effective concentration.


The Journal of Steroid Biochemistry and Molecular Biology | 2010

Identification and Characterization of an Androgen-responsive Kap Promoter Enhancer Located in the Intron II Region of human Angiotensinogen Gene

Li-Qiang Fan; Dianne O. Hardy; James F. Catterall; Jian Zhao; Su-Xia Li

Transgenic expression of the human angiotensinogen (HAGT) gene directed by the mouse kidney androgen-regulated protein (Kap) gene promoter is proximal tubule cell-specific and androgen-regulated in vivo. The same Kap promoter fragment did not support similar regulation of other genes, but a transgene based on the original chimeric KAP-hAGT construct successfully directed NHE3 to kidney, suggesting that sequences within the HAGT gene fragment of the construct contributed to the regulation of its expression in vivo. In the present study, androgen-responsive regulatory sequences in the HAGT gene portions of the transgene were examined in transfected renal cells. A 1.4-kb enhancer between exons 2 and 3 was identified that increased the basal expression of Kap promoter 1.5- to 2-fold, its induction by dihydrotestosterone (DHT) 2- to 3-fold and its induction by dexamethasone (Dex) 4- to 5-fold. Sequence analysis revealed two potential hormone-responsive elements. Mutational assays and electrophoretic mobility shift assay showed one of these elements was androgen-specific. These findings may influence future strategies for the design of inducible, cell-specific transgenes.


Applied Biochemistry and Biotechnology | 2014

Essential Role of Gly33 in a Novel Organic Solvent-Tolerant Lipase from Serratia marcescens ECU1010 as Determined by Site-Directed Mutagenesis

Su-Xia Li; Qiang Ma; Kang Lin; Jiao-Jiao Wu; Yixin Wu; Jian-He Xu

A novel lipase lipB from Serratia marcescens ECU1010 is highly stable in the presence of organic solvents. By sequence and structure comparison with homologous lipase lipA, three amino acid residues were found to be different between them. To identify the residues which increase the organic solvent stability of lipB, residues that potentially provide this stability were mutated to the ones of lipA at equivalent positions. The replacement of Gly at position 33 by Asp obviously decreased its stability in organic solvents. Molecular modeling and structural analysis also suggested that the Gly33 residue is important for the organic solvent stability of lipB.


Enzyme and Microbial Technology | 2011

Increasing the refolding efficiency in vitro by site-directed mutagenesis of Cys383 in rat procarboxypeptidase B.

Su-Xia Li; Luosheng Zhang; Qian Wu; Aijie Xin; Jian Zhao; Li-Qiang Fan

This study examines a novel method to reduce the probability of disulfide mismatches during the refolding process by the replacement of cysteines within a protein. Specifically, Cys383 of recombinant rat procarboxypeptidase B was replaced by other amino acids to increase the refolding efficiency in vitro. Mutants C383G, C383A and C383S could refold successfully, but mutants C383R, C383E, C383L and C383Y failed to refold correctly. Compared with wild type, the refolding efficiencies of mutants C383G and C383A were enhanced. The Cys383 mutations changed some of the properties of rat carboxypeptidase B. Mutants C383G, C383A had higher k(cat)/K(m) values which indicated increased catalytic abilities. And both had higher thermal stability. pH had different effects on the activities and stabilities of the mutant and wild type proteins. The studies suggested that mutating Cys383 of rat procarboxypeptidase B could improve the renaturation process by increasing the refolding efficiency. This new method could be taken as a new attempt to improve the refolding efficiency of other recombinant proteins containing disulfide bonds that are expressed as inclusion bodies. While the results also claimed that the potential effects of the substituted amino acid on the protein itself should be seriously considered in addition to its ability to reduce the probability of disulfide mismatches.


Applied Biochemistry and Biotechnology | 2011

Expression and characterization of a novel lipase from Aspergillus fumigatus with high specific activity.

Jiao-Jiao Shangguan; Yu-Qiang Liu; Fu-Jun Wang; Jian Zhao; Li-Qiang Fan; Su-Xia Li; Jian-He Xu


Food Chemistry | 2007

Effect of multiple factors on accumulation of nucleosides and bases in Cordyceps militaris

Yuxiang Gu; Zunsheng Wang; Su-Xia Li; Qinsheng Yuan


Enzyme and Microbial Technology | 2005

Purification and partial characterization of Cu, Zn containing superoxide dismutase from entomogenous fungal species Cordyceps militaris

Zunsheng Wang; Zhuojing He; Su-Xia Li; Qinsheng Yuan


Applied Biochemistry and Biotechnology | 2010

Significantly Improved Expression and Biochemical Properties of Recombinant Serratia marcescens Lipase as Robust Biocatalyst for Kinetic Resolution of Chiral Ester

Yi Wang; Jian Zhao; Jian-He Xu; Li-Qiang Fan; Su-Xia Li; Li-Li Zhao; Xiao-Bo Mao


Applied Microbiology and Biotechnology | 2014

Heterologous overexpression of Vigna radiata epoxide hydrolase in Escherichia coli and its catalytic performance in enantioconvergent hydrolysis of p-nitrostyrene oxide into (R)-p-nitrophenyl glycol

Qing-Qing Zhu; Wanhong He; Xu-Dong Kong; Li-Qiang Fan; Jian Zhao; Su-Xia Li; Jian-He Xu


Applied Biochemistry and Biotechnology | 2013

Production, Characterization, and Application of an Organic Solvent-Tolerant Lipase Present in Active Inclusion Bodies

Su-Xia Li; Kang Lin; Huaiyu Pang; Yixin Wu; Jian-He Xu

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Jian Zhao

East China University of Science and Technology

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Li-Qiang Fan

East China University of Science and Technology

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Qinsheng Yuan

East China University of Science and Technology

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Jian-He Xu

East China University of Science and Technology

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Zunsheng Wang

East China University of Science and Technology

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Kang Lin

East China University of Science and Technology

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Qiong Shen

East China University of Science and Technology

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Yi Gong

Chinese Academy of Sciences

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Zhuojing He

East China University of Science and Technology

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