The title compound, 5Ni%propyl2(2′nitrobenzenesulfonyl)glutamine, was synthesized and its structure was confirmed by IR, MS, {}~1H NMR, and elemental analysis. The single crystal structure of the title compound was determined by Xray diffraction. The crystal belongs to Monoclinic, space group %P%2(1), with a=0.69281(11) nm, b=0.76508(12), c=1.5843(3) nm, α=90°, β=90.941(3)°, γ=90°, V=0.8397(2) nm^3, Z=2, D-c=1.477 g/cm^3, μ=0.236 mm~ -1 , F(000)=392, R=0.0297, and wR=0.0664.
XIAO Yong-jun WANG Jian-guo WANG Bao-lei LI Zheng-ming SONG Hai-bin
2-Chloro-N-{2-fluoro-5-[N-(phenylsulfonyl)phenylsulfonamido]phenyl}benzamide was synthesized and its crystal structure was also determined by X-ray single-crystal diffraction. The title compound(C25H18ClFN2O5S2) belongs to monoclinic, space group P21/n with a=0.7377(3) nm, b=1.2036(5) nm, c=2.6846(11) nm, β=90.895(9)°, V=2.3833(16) nm3, Mr=544.98, Z=4, Dc=1.519 g/cm3, μ=0.385 mm–1, F(000)=1120, R1=0.0632, and wR2=0.1438. Its crystal structure belongs to a novel class that has not been reported yet, and its preliminary herbicidal activity was also tested. Its inhibition rate to seedling growth of barnyard grass reaches 15.1% at 100 μg/mL.
LI Wen-ming WANG Jian-guo LI Zheng-ming SONG Hai-bin
Introduction Nerve growth factor(NGF) was first discovered and purified by Rita Levi-Montalcini and Stanley Cohen in the 1950s[1,2]. It represents the first cellular growth factor ever discovered and involved in the growth, survival, and differentiation of specific nerve cell popula-tions[3].
The entire gene of carboxyltransferase(CT) domain of acetyl-CoA carboxylase(ACCase) from Chinese Spring wheat(CSW) plastid was cloned firstly, and the 2.3 kb gene was inserted into PET28a+ vector and expressed in E. coil in a soluble state. The (His)6 fusion protein was identified by SDS-PAGE and Western blot. The recombinant protein was purified by affinity chromatography, and the calculated molecular mass(Mr) was 88000. The results of the sequence analysis indicate that the cloned gene(GeneBank accession No. EU124675) was a supplement and revision of the reported ACCase CT partial cDNA from Chinese Spring wheat plastid. The recombinant protein will be significant for us to investigate the recognizing mechanism between ACCase and herbicides, and further to screen new herbicides.
WANG Rui-jianYANG Xue-yingZHENG Liang-yuYANG YeGAO GuiCAO Shu-gui
Acetyl-CoA carboxylase(ACCase) is a crucial enzyme in fatty acid synthesis, by regulating the first committed step in the process. Therefore, it is a potential target for the development of new compounds against obesity or as herbicides. The cDNA encoding yeast ACCase CT domains(YCTs) from Saccharomyces cerevisiae was amplified by RT-PCR and inserted into the vector PET28a(+) for bacterial expression of YCT fused to N-terminal His-tag(YCT-his6). YCTs-his6 was expressed in Escherichia coli BL21(DE3) PLys as inclusion bodies, which was solubilized in 8 mol/L urea. Ni-agarose chromatography was used to purify the inclusion bodies under denaturing condition. Correct refolding was achieved via systematic dialysis to remove the denaturant gently in the presence of 0.5 mmol/L Triton X-100. The low concentration Triton X-100 was included in the refolding buffer to increase the solubilization and enhance dimeric formation of refolding proteins. The activity of the refolded YCT-his6 was 1.2 U/mg as measured in a spectrophotometric assay using malonyl-CoA as the substrate. To our knowledge, it is the first time that the bioactive YCT-his6 has been expressed successfully in E. coli and isolated from their inclusion bodies.
YANG Xue-ying TAO Jin ZHENG Liang-yu WANG Rui-jian ZHAO Ke CAO Shu-gui
