Search Results
You are looking at 1 - 5 of 5 items for
- Author or Editor: S. G. Yuan x
- Refine by Access: All Content x
Abstract
During a five-year period, the International Atomic Energy Agency supported a Coordinated Research Programme (CRP) to investigate the quantitative relationship between internal body burdens of a number of elements of environmental health significance and their respective concentrations in hair. The use of nuclear-related analytical techniques, such as neutron activation analysis, X-ray fluorescence, particle-induced X-ray emission and radiotracers, was emphasized. One aspect of the CRP focused on studies in man, using autopsy cases, of mineral distribution in five tissues, i.e. liver, kidney, lung, brain and bone in addition to hair, and the elements of primary importance were As, Cd, Cu, Hg, Pb, Se and Zn. Emphasis was placed on analytical quality assurance. Hair and internal tissue samples were obtained from subjects from Bulgaria, China, the former German Democratic Republic, Hungary, Japan, Norway and Sweden.
Summary
The extraction of protactinium with Aliquat 336 (methyl-tri-caprylyl ammonium chloride) in toluene, cyclohexane and chloroform from HCl, HNO3, H2SO4, HClO4, HF and mixed HCl-HF media was investigated by radioactive tracer technique. Distribution ratios of protactinium between the aqueous solution and the organic phase were determined as a function of shaking time, concentrations of acid in aqueous solution phase, extractant concentration and type of diluents in the organic phase. Aliquat 336 can almost quantitatively extract protactinium from strong HCl solution. At the same time, small amounts of HF in HCl solutions have a strong effect on Pa distribution.
Seven Glu-A1 m allelic variants of the Glu-A1 m x genes in Triticum monococcum ssp. monococcum, designated as 1Ax2.1 a , 1Ax2.1 b , 1Ax2.1 c , 1Ax2.1 d , 1Ax2.1 e , 1Ax2.1 f , and 1Ax2.1 g were characterized. Their authenticity was confirmed by successful expression of the coding regions in E. coli, and except for the 1Ax2.1 a with the presence of internal stop codons at position of 313 aa, all correspond to the subunit in seeds. However, all the active six genes had a same DNA size although their encoding subunits showed different molecular weight. Our study indicated that amino acid residue substitutions rather than previously frequently reported insertions/deletions played an important role on the subunit evolution of these Glu-A1 m x alleles. Since variation in the Glu-A1x locus in common wheat is rare, these novel genes at the Glu-A1 m x can be used as candidate genes for further wheat quality improvement.
High-molecular-weight glutenin subunits (HMW-GSs) are important seed storage proteins associated with bread-making quality in common wheat (Triticum aestivum L., 2n = 6x = 42, AABBDD). Variation in the Glu-A1x locus in common wheat is scare. Diploid Triticum monococcum ssp. monococcum (2n = 2x = 14, AmAm) is the first cultivated wheat. In the present study, allelic variations at the Glu-A1 m x locus were systematically investigated in 197 T. monococcum ssp. monococcum accessions. Out of the 8 detected Glu-A1 m x alleles, 5 were novel, including Glu-A1 m -b, Glu-A1 m -c, Glu-A1 m -d, Glu-A1 m -g, and Glu-A1 m -h. This diversity is higher than that of common wheat. Compared with 1Ax1 and 1Ax2*, which are present in common wheat, these alleles contained three deletions/insertions as well as some single nucleotide polymorphism variations that might affect the elastic properties of wheat flour. New variations in T. monococcum probably occurred after the divergence between A and Am and are excluded in common wheat populations. These allelic variations could be used as novel resources to further improve wheat quality.
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.
