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Wyszukujesz frazę "Zhang, Xin" wg kryterium: Autor


Wyświetlanie 1-4 z 4
Tytuł:
Human neutrophil peptide 3 could be functionally expressed in Rhodobacter sphaeroides
Autorzy:
Nie, Xin
Zhang, Li
Hu, Zongli
Liu, Yi
Zhao, Zhiping
Powiązania:
https://bibliotekanauki.pl/articles/1039101.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Rb. sphaeroides
HNP3
expression system
antimicrobial activity
spectral absorption
Opis:
Human neutrophil peptides (HNPs) possess high antimicrobial activities against a broad spectrum of microorganisms. Rhodobacter sphaeroides is the best-characterized photosynthetic bacterium and exhibits potential as a novel expression system. Up to date, no literature has been reported regarding expression of HNP3 in Rb. sphaeroides. In the present study, the HNP3 gene fragment was amplified by SOE PCR and ligated into photosynthetic bacteria light-harvesting complex 2 (LH2) expression vector leading to HNP3 fusion protein expression vector. The HNP3 fusion protein was successfully expressed as rapidly evaluated by the LH2 characteristic peaks at ~800 nm and ~850 nm before purification and SDS/PAGE. Subsequently, the HNP3 fusion protein was purified by one-step affinity chromatography, and could be rapidly detected by the color and the spectral absorption at ~800 nm and ~850 nm before SDS/PAGE. Antimicrobial activity assay suggested that the HNP3 fusion protein exhibited high antimicrobial activity towards E. coli. The present study may supply an insight into employing the novel Rb. sphaeroides expression system, exhibiting dramatic advantages over currently used commercial expression system, to heterologously express human neutrophil peptides.
Źródło:
Acta Biochimica Polonica; 2015, 62, 2; 259-263
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
High-grade mutant OmpF induces decreased bacterial survival rate
Autorzy:
Zhao, Zhi-ping
Liu, Ting-ting
Zhang, Li
Luo, Min
Nie, Xin
Li, Zai-xin
Pan, Yu
Powiązania:
https://bibliotekanauki.pl/articles/1039304.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
antibiotic resistance
mOmpF
OmpF
outer membrane protein
bacterial survival rate
Opis:
OmpF plays very important roles in the influx of antibiotics and bacterial survival in the presence of antibiotics. However, high-grade mutant OmpF and its function in decreasing bacterial survival rate have not been reported to date. In the present study, we cloned a high-grade mutant OmpF (mOmpF) and sequence analysis suggested that over 45 percent of the DNA sequence was significantly mutated, leading to dramatic changes in over 55 percent of the amino acid sequence. mOmpF protein was successfully expressed. When grown in the presence of antibiotic, the bacterial survival rate decreased and the antibiotic inhibition zone became larger with the increase of the mOmpF. It was concluded that concentration of high-grade mutant mOmpF dramatically influenced the bacterial survival rate. The study presented here may provide insights into better understanding of the relationships between structure and function of OmpF.
Źródło:
Acta Biochimica Polonica; 2014, 61, 2; 369-373
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Molecular cloning and expression analysis of a new gene for short-chain dehydrogenase/reductase 9
Autorzy:
Liu, Shen
Huang, Chaoqun
Li, Dawei
Ren, Weihua
Zhang, Haoxing
Qi, Meiyan
Li, Xin
Yu, Long
Powiązania:
https://bibliotekanauki.pl/articles/1041143.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
liver
clone
short-chain dehydrogenase/reductase
Opis:
We report here the cloning and characterization of a novel human short-chain dehydrogenases/reductase gene SCDR9, isolated from a human liver cDNA library, and mapped to 4q22.1 by browsing the UCSC genomic database. SCDR9 containing an ORF with a length of 900 bp, encoding a protein with a signal peptide sequence and an adh_short domain. GFP localization shows SCDR9 protein concentrated in some site of the cytoplasm, but not in the ER. Expression pattern in eighteen tissues revealed that SCDR9 is expressed highly in liver. Soluble recombinant protein was successfully purified from Escherichia coli using pET28A(+) expression vector. Our data provides important information for further study of the function of the SCDR9 gene and its products.
Źródło:
Acta Biochimica Polonica; 2007, 54, 1; 213-218
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.
Autorzy:
Zhang, Jiayi
Dai, Jianliang
Zhao, Enpeng
Lin, Yun
Zeng, Li
Chen, Jinzhong
Zheng, Huari
Wang, Yu
Li, Xin
Ying, Kang
Xie, Yi
Mao, YuMin
Powiązania:
https://bibliotekanauki.pl/articles/1041522.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ovary
ePAD
peptidylarginine deiminase
hPADVI
Opis:
Peptidylarginine deiminase (PAD) catalyzes the post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Human, similar to rodents, has four isoforms of PAD (type I, II, III and IV/V), each of which is distinct in substrate specificity and tissue specific expression. In our large-scale sequencing project, we identified a new human PAD cDNA from a human fetal brain cDNA library. The putative protein encoded by this cDNA is designated hPADVI. Expression analysis of hPADVI showed that it is mainly expressed in adult human ovary and peripheral blood leukocytes. We conclude that hPADVI may be orthologous to mouse ePAD, basing on sequence comparison, chromosome localization and exon-intron structure analysis. PAD-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development. This study describes a new important member of the human PAD family.
Źródło:
Acta Biochimica Polonica; 2004, 51, 4; 1051-1058
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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