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Abstract  

To increase the tumor uptake of Val-Gly-Gly (VGG), adenine was introduced into the peptide. N-mercaptoacetyl-VGG-adenine (MAVGG-adenine) and MAVGG were labeled with 99mTc using a solution of SnCl2 and tartaric acid as reducing agent. Biodistribution in mice bearing the S180 tumor was measured and γ imaging was performed. Compared with MAVGG, adenine conjugated MAVGG had higher tumor uptake and tumor to normal tissue ratios, which suggested that the tumor uptake property of a peptide may be improved by introducing a nucleotide base. The high contrasted tumor images of 99mTc-MAVGG-adenine also suggested its potential utility as tumor imaging agent.

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Abstract  

Two peptide ligands conjugated adenine, [9-N-(tritylmercapto acetyl diglycyl aminoethyl) adenine, Tr-MAG2-Ade] and [9-N-(tritylmercapto acetyl triglycyl aminoethyl) adenine, Tr-MAG3-Ade], are synthesized and labeled with 99mTc by directly labeling method. The stability of 99mTc-MAG2-adenine and 99mTc-MAG3-adenine in vitro is measured. The uptake radios of tumor to muscle at 3h post-injection are 5.70 and 4.92, respectively. The biodistribution and scintigraphic imaging studies show that the two complexes have high localization in tumor and high contrasted tumor images can be obtained, which suggest their potential utility as tumor imaging agents. But the high radioactivity of abdomen could prevent the tumor imaging in this area.

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Wheat-rye 1BL.1RS translocations have been widely used in wheat breeding programs. A 1BL.1RS translocation wheat line, 91S-23, was developed from a 1R monosomic addition of the rye (Secale cereale) inbred line L155 into wheat (Triticum aestivum) MY11. A new commercial wheat cultivar, CN18, which also contained the 1BL.1RS translocation, was derived from the cross MY11 × 91S-23. Polymerase chain reaction (PCR) and fluorescence in situ hybridization (FISH) indicated that the rye centromere was eliminated from the 1BL.1RS chromosomes of CN18 but not from 91S-23. Based on the 1RS source and the centromeric structure of the translocation chromosome, CN18 qualifies as a new wheat cultivar possessing a 1BL.1RS translocation. CN18 displayed high yield performance and resistance to powdery mildew and stripe rust, whereas 91S-23 was susceptible to these diseases. The present study provides a new 1RS resource for wheat improvement.

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Fluorescence in situ hybridization (FISH) can reveal minor structural differences of chromosomes. The karyotype of common wheat (Triticum aestivum L.) based on FISH pattern is seldom reported. In this study, non-denaturing FISH (ND-FISH) using Oligo-pSc119.2-1, Oligo-pTa535-1 and (AAG)6 as probes was used to investigate the chromosomal structure of 85 common wheat including 83 wheat-rye 1RS.1BL translocation cultivars/lines, a wheatrye 1RS.1AL translocation cultivar Amigo and Chinese Spring (CS). Two, three, two, three, six, three and four structural types respectively for 1A, 2A, 3A, 4A, 5A, 6A and 7A chromosomes were observed. Two, eight, two, two, four and six types of chromosome for 2B, 3B, 4B, 5B, 6B and 7B were respectively detected. The structure of 1B chromosomes in Amigo and CS is different. Five, two, two and two types of chromosomal structure respectively for 1D, 2D, 3D and 5D were distinguished. Polymorphisms of 1RS.1BL, 4D, 6D and 7D chromosomes were not detected. Chromosomes 1AI, 2AI, 3AI, 4AI, 5AIII, 6AI, 7AIII, 2BI, 3BV, 4BI, 5BII, 6BIII, 7BI, 1DIV, 2DI, 3DI and 5DII appeared in these 85 wheat cultivars/lines at high frequency. Each of the 85 wheat cultivars/lines has a unique karyotype. Amigo is a complex translocation cultivar. The FISH karyotype of wheat chromosomes built in this study provide a reference for the future analyzing wheat genetic stocks and help to learn structural variations of wheat chromosomes. In addition, the results in this study indicate that oligonucleotide probes and ND-FISH technology can be used to identify individual wheat cultivar.

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Abstract  

A novel double -diketone 1,6-bis(1-phenyl-3-methyl-5-oxo-pyrazol-4-yl) hexanedione-[1,6] (BPMOPH) was further studied on its coordination compounds with uranium and thorium, respectively. The IR, UV, and1H-NMR spectra were examined, and the proposed structure is discussed.

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Cereal Research Communications
Authors: G. Chen, M.H. Zhang, X.J. Liu, J.Y. Fu, H.Y. Li, M. Hao, S.Z. Ning, Z.W. Yuan, Z.H. Yan, B.H. Wu, D.C. Liu, and L.Q. Zhang

Premature termination codons (PTCs) are an important reason for the silence of highmolecular- weight glutenin subunits in Triticum species. Although the Glu-A1y gene is generally silent in common wheat, we here isolated an expressed Glu-A1y gene containing a PTC, named 1Ay8.3, from Triticum monococcum ssp. monococcum (AmAm, 2n = 2x = 14). Despite the presence of a PTC (TAG) at base pair positions 1879–1881 in the C-terminal coding region, this did not obviously affect 1Ay8.3 expression in seeds. This was demonstrated by the fact that when the PTC TAG of 1Ay8.3 was mutated to the CAG codon, the mutant in Escherichia coli bacterial cells expressed the same subunit as in the seeds. However, in E. coli, 1Ay8.3 containing the PTC expressed a truncated protein with faster electrophoretic mobility than that in seeds, suggesting that PTC translation termination suppression probably occurs in vivo (seeds) but not in vitro (E. coli). This may represent one of only a few reports on the PTC termination suppression phenomenon in genes.

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