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1

Purification and characterization of two extracellular lipases from Pseudomonas aeruginosa Ps-x

100%
Saeed H. M., Zaghloul T. I., Khalil A. I., Abdelbaeth M. T.
Polish Journal of Microbiology
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2005
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tom 54
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nr 3
Two different extracellular lipases were isolated and purified from Pseudomonas aeruginosa Ps-x to apparent homogeneity using ammonium sulfate precipitation followed by ion exchange chromatography on Q- and S-Sepharose column. Both of the purified lipases are monomeric protein with molecular weight of 15.5 and 54.97 KDa respectively. The optimal activities of the enzymes were at 45 and 50°C and pHs 10.0 and 9.0. Calcium ions increase thermostability of both purified lipases I and II. The purified lipase I showed no metal ion dependence for its activity since EDTA up to 10 mM has no effect on the enzyme activity. However purified lipase II showed slight inhibition by EDTA at the same concentration. Moreover, a serine protease inhibitor, PMSF showed an inhibitoiy effect on both purified enzymes.
2

Purification and characterization of extracellular Pseudomonas aeruginosa urate oxidase enzyme

100%
Saeed H. M., Abdel-Fattahyousry Y. R., Gohar M., Elbaz M. A.
Polish Journal of Microbiology
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2004
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tom 53
|
nr 1
Urate oxidase (uricase) was isolated and purified from Pseudomonas aeruginosa to apparent homogeneity using ammonium sulphate precipitation followed by ion exchange and gel filtration chromatography. The specific activity of the purified uricase enzyme was found to be 636.36 with the use of uric acid as a substrate. The purified uricase enzyme is a monomeric protein with molecular weight of 64 kilodaltons. The optimal pH and temperature of the purified enzyme is 9.0 and 30°C, respectively. The effect of some metal ions was studied. Sulphate forms of Fe⁺², Zn⁺² and Co⁺² inhibit the uricolytic activity whereas; NaCl and CaCl₂ enhance the enzyme activity. Moreover, the purified enzyme is inhibited by EDTA and KCN.
3

Identification, cloning and expression of Pseudomonas aeruginosa Ps-x putative urate oxidase gene in Escherichia coli

88%
Saeed H. M., Abdel-Fattah Y. R., Berekaa M. M., Gohar Y. M., Elbaz M. A.
Polish Journal of Microbiology
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2004
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tom 53
|
nr 4
In a previous study we reported for the first time the isolation and characterization of urate oxidase enzyme from Pseudomo-nas aeruginosa. In this work we isolated and cloned a 1.350 kilobase DNA fragment that encode a putative urate oxidase gene from the genomic library of P. aeruginosa Ps-x. The nucleotide sequence of the cloned DNA insert revealed an open reading frame that encodes a protein of a molecular weight of 54.0 kDa. The cloned DNA fragment showed an uricolytic activity when expressed in E. coli DH5α . Surprisingly, the nucleotide sequence of the cloned gene showed more than 99% identity to the gene encoding hypothetical protein of P. aeruginosa PAO1. Moreover, the sequence of the cloned gene was closely similar to the corresponding unease gene of Cellulomonas Jlavigena (44% similarity), but showed lower similarity values to that of Bacillus sp. BT-90 (24% similarity), Candida utilis (24% similarity). Interestingly, the isolated uricase gene showed closer similarity to uricase from yeast-like symbiotic fungi Beauveria bassiana (35%), Tolypocladium inflatum (29%), Paecilomyces tenuipes (27%) and Cerataphis fransseni (24%).
4

Matrix metalloproteinase-2 C-1306T promoter polymorphism and breast cancer risk in the Saudi population

76%
Saeed H. M., Alanazi M. S., Alshahrani O., Parine N. R., Alabdulkarim H. A., Shalaby M. A.
Acta Biochimica Polonica
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2013
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tom 60
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nr 3
Matrix metalloproteinase-2 (MMP-2) is an enzyme with proteolytic activity against matrix proteins, particularly basement membrane constituents. A single nucleotide polymorphism (SNP) at -1306, which disrupts a Sp1-type promoter site (CCACC box), displayed a strikingly lower promoter activity with the T allele. In the present study, we investigate whether this MMP-2 SNP is associated with susceptibility to breast cancer in the Saudi population. Ninety breast cancer patients and 92 age matched controls were included in this study. TaqMan Allele Discrimination assay and DNA sequencing techniques were used for genotyping. The results showed that, the frequency of MMP-2 CC wild genotype was lower in breast cancer patients when compared with healthy controls (0.65 versus 0.79). The homozygous CC (OR=2, χ2=5.36, p=0.02) and heterozygous CT (OR=1.98, χ2=4.1, p=0.04) showing significantly high risk of breast cancer in the investigated group. In conclusion our data suggest that the MMP-2 C-1306T polymorphism may be associated with increased breast cancer risk in the Saudi population.
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