Name | Guanosine triphosphate |
Synonyms | 5'-GTP Guo-5'-P3 Guanosine triphosphate D-Guanosine5'-triphosphate guanosine triphosphate (-Na2) Guanosine 5'-triphosphoric acid guanosine 5'-(tetrahydrogen triphosphate) [(2R,3S,4R,5R)-5-(2-amino-6-oxo-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl (hydroxy-phosphonooxyphosphoryl) hydrogen phosphate |
CAS | 86-01-1 |
EINECS | 201-647-3 |
Molecular Formula | C10H16N5O14P3 |
Molar Mass | 523.18 |
Density | 2.75±0.1 g/cm3(Predicted) |
pKa | pK3:3.0(-2);pk5:7.10(-3);pK6:9.3(-4) (25°C,μ=0.1) |
Physical and Chemical Properties | This product is white or off-white powder, odorless, with hygroscopicity. Soluble in water, in alcohol, chloroform insoluble. |
Author:
Zongfeng ,< a href = "https://xueshu.baidu.com/usercenter/data/author?cmd=authoruri&wd=authoruri:(5 bd37da2f3c91921) author:(Ding Guoxian)" target = "_blank"> Ding Guoxian ,< a href = "https://xueshu.baidu.com/usercenter/data/author?cmd=authoruri&wd=authoruri:(41800486 f29937e1) author:(Cheng Yunlin)" target = "_blank">
Summary:
objective: to investigate the expression of 8-hydroxy -2 '-deoxyguanosine triphosphate (8-oxo-dGTPase) and the changes of telomere length when human peripheral blood lymphocytes are injured by H2O2, and to evaluate the effect of oxidative stress on telomere length. Methods: Human peripheral blood lymphocytes were cultured in vitro and divided into normal control group, oxidation group and antioxidant group. Semi-quantitative reverse transcription polymerase chain reaction (RT-PCR) and gel imaging technology were used to determine the mRNA expression level of 8-oxo-dGTPase, and the changes of telomere length were detected by Southern hybridization technology. Results: ① With the extension of H2O2 action time, the relative content of 8-oxo-dGTPasemRNA also increased, especially in the oxidation group (P0.05), while there was no significant difference between the antioxidant group and the control group (P0.05). ② Telomere length decreased with time
keywords:
lymphocyte oxidative stress 8-hydroxy -2 & prime;-deoxyguanosine triphosphate telomere length immune aging
DOI:
10.3969/j.issn.1007-4368.2005.04.016
cited:
Year:
2005
Zhao Guixian ,< a href = "https://xueshu.baidu.com/usercenter/data/author?cmd=authoruri&wd=authoruri:(65 e3fcc2dfa41b38) author:(Wu Zhiying)" target = "_blank"> Wu Zhiying ,< a href = "https://xueshu.baidu.com/usercenter/data/author?cmd=authoruri&wd=authoruri:(4 c194cc7df7420c4) author:(Chen Wanjin)" target = "_blank"> Chen wanjin ,< a href = "https://xueshu.baidu.com/usercenter/data/author?cmd=authoruri&wd=authoruri:(8 d2aad2666514ed5) author:(Lin yi)" target = "_blank"> Lin yi ,< a href = "https://xueshu.baidu.com/usercenter/data/author?cmd=authoruri&wd=authoruri:(7 a43f52a661150a4) author:(Wang ning)" target = "_blank"> Wang ning
Summary:
objective: to express the full-length fusion protein of human immune-related guanosine triphosphate gene (IRGM)a and prepare high-quality rabbit anti-human IRGM polyclonal antibody. Methods: IRGMa full-length cDNA fragments were cloned into prokaryotic expression vector pGEX-4T-2 and eukaryotic expression vector pCMV-myc respectively, and the sequence was verified to be correct by sequencing. The IRGMa/GST fusion protein was expressed in E.coli BL21, and purified soluble IRGMa/GST fusion protein was used to immunize New Zealand white rabbits to prepare rabbit anti-human IRGM antibody. ELISA, immunoblotting and competitive inhibition were used to verify its sensitivity and specificity. Results: The specificity and sensitivity of self-made rabbit anti-human IRGM polyclonal antibody were higher, and the titer was higher than that of commercial antibody. Conclusion: Rabbit anti-human IRGM polyclonal antibody has been successfully prepared, which lays a foundation for further functional research.
keywords:
immune-related guanosine triphosphate gene fusion protein polyclonal antibody
DOI:
CNKI:SUN:LCSK. 0.2009-06-011
Year:
2009