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Summary  

The comprehension of the behavior of radioactive nuclides in aquifer requires the study of the sorption processes of nuclides in various geochemical conditions. The sorption/desorption of 65Zn(II) on surface sediments (0-2 cm) was investigated by batch method in sea water (pH 8.20, 35‰ salinity, filtered by 0.45mm) at ambient temperature. The surface sediments were obtained from four stations around the Daya Bay of Guangdong Province (China), where the first nuclear power station of China has been running from 1994. The sorption process is fast initially and around 39% average of sorption percentage (SP%) can be quickly obtained in 15 minutes for all the surface sediments. Then, the sorption percentage becomes constant. In 30 days of contact time 79.6% sorption percentage and K d=3.9. 103ml/g distribution coefficient was obtained. The value of K dbecame constant, 4.0. 103ml/g, in contact time more than 120 hours. The distribution coefficient K ddecreases with increasing sediment concentration from 4.0 to 250 mg/l from 1.31. 104to 1.68. 103ml/g, respectively. Then the value of K dgoes up to 5.38. 103ml/g with sediment concentration of 3000 mg/l. The desorption experiments suggest that the sorption of Zn(II) is irreversible with a hyteresis coefficient of 66%.

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New high-molecular-weight glutenin (HMW glutenin) sequences isolated from six Psathyrostachys juncea accessions by thermal asymmetric interlaced PCR differ from previous sequences from this species. They showed novel modifications in all of the structural domains, with unique C-terminal residues, and their N-terminal lengths were the longest among the HMW glutenins reported to date. In their repetitive domains, there were three repeatable motif units: 13-residue [GYWH(/I/Y)YT(/Q)S(/T)VTSPQQ], hexapeptide (PGQGQQ), and tetrapeptide (ITVS). The 13-residue repeats were restricted to the current sequences, while the tetrapeptides were only shared by D-hordein and the current sequences. However, these sequences were not expressed as normal HMW glutenin proteins because an in-frame stop codon located in the C-termini interrupted the intact open reading frames. A phylogenetic analysis supported different origins of the P. juncea HMW glutenin sequences than that revealed by a previous study. The current sequences showed a close relationship with D-hordein but appeared to be more primitive.

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Cereal Research Communications
Authors:
S.F. Dai
,
D.Y. Xu
,
Z.J. Wen
,
Z.P. Song
,
H.X. Chen
,
H.Y Li
,
J.R. Li
,
L.Z. Kang
, and
Z.H. Yan

A novel 4.0-kb Fy was sequenced and bacterially expressed. This gene, the largest y-type HMW-GS currently reported, is 4,032-bp long and encodes a mature protein with 1,321 amino acid (AA) residues. The 4.0-kb Fy shows novel modifications in all domains. In the N-terminal, it contains only 67 AA residues, as three short peptides are absent. In the repetitive domain, the undecapeptide RYYPSVTSPQQ is completely lost and the dodecapeptide GSYYPGQTSPQQ is partially absent. A novel motif unit, PGQQ, is present in addition to the two standard motif units PGQGQQ and GYYPTSPQQ. Besides, an extra cysteine residue also occurs in the middle of this domain. The large molecular mass of the 4.0-kb Fy is mainly due to the presence of an extra-long repetitive domain with 1,279 AA residues. The novel 4.0-kb Fy gene is of interest in HMW-GS gene evolution as well as to wheat quality improvement with regard to its longest repetitive domain length and extra cysteines residues.

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